rasG

UniProt ID: P15064
Organism: Dictyostelium discoideum
Review Status: COMPLETE
📝 Provide Detailed Feedback

Gene Description

RasG (DdrasG) is the most abundant Ras subfamily small GTPase in growing Dictyostelium discoideum and the closest amoebozoan relative of mammalian K-Ras. Like other Ras proteins it is a C-terminally prenylated, plasma-membrane-anchored molecular switch that cycles between an inactive GDP-bound and an active GTP-bound state, controlled by guanine-nucleotide exchange factors (RasGEFs such as GefR/Aimless) and GTPase-activating proteins (RasGAPs such as NF1, IqgC, C2GAP1 and the Leep2 complex). Upon chemoattractant (folate or cAMP) stimulation, RasG is rapidly and transiently activated at the leading edge and cell cortex, where GTP-loaded RasG binds and activates class I phosphatidylinositol 3-kinase to generate PIP3, driving F-actin-based pseudopod formation, directional sensing and cell motility. RasG is a principal regulator of chemotaxis, random motility and cell polarity, cytokinesis, macropinocytosis and phagocytosis, engaging effectors including PI3K, the Diaphanous-related formin ForG, the NDR/LATS kinase NdrC, TORC2, the Ras-interacting protein RIP3/RipA and the MRL-family adaptor DydA. Its functions overlap partly with the paralogs RasC (more specialized for cAMP relay and adenylyl cyclase activation) and RasD (which can substitute for RasG in cytokinesis).

Existing Annotations Review

GO Term Evidence Action Reason
GO:0003924 GTPase activity
IBA
GO_REF:0000033
ACCEPT
Summary: Phylogenetic inference that RasG has intrinsic GTPase activity. This is the defining catalytic property of a Ras-family small GTPase and is directly supported for RasG (EC 3.6.5.2, GTP hydrolysis inactivates the switch).
Reason: RasG is a bona fide Ras GTPase that hydrolyzes GTP to GDP; the intrinsic GTPase activity is a core molecular function and is well conserved across the family.
Supporting Evidence:
PMID:15143344
the subsequent inactivation is due to an enhancement of the intrinsic GTPase activity, which is stimulated by the GTPase-activating proteins (GAPs)
GO:0005886 plasma membrane
IBA
GO_REF:0000033
ACCEPT
Summary: Phylogenetic inference of plasma membrane localization, corroborated by direct imaging of GFP-RasG uniformly distributed along the plasma membrane and activated at the cortex/leading edge.
Reason: RasG is prenylated and anchored to the cytoplasmic face of the plasma membrane, where it is activated and signals; this is a core localization.
Supporting Evidence:
PMID:15534002
GFP-RasG displayed uniform localization along the plasma membrane and cytosol
GO:0007264 small GTPase-mediated signal transduction
IBA
GO_REF:0000033
ACCEPT
Summary: Phylogenetic inference that RasG participates in small GTPase-mediated signal transduction. This is the core signaling role of RasG as a molecular switch relaying chemoattractant signals to PI3K and other effectors.
Reason: RasG functions as a GTP/GDP molecular switch in signal transduction, a core function directly demonstrated experimentally.
Supporting Evidence:
PMID:15534002
Ras is rapidly and transiently activated in response to chemoattractant stimulation and regulates PI3K activity
GO:0000281 mitotic cytokinesis
IBA
GO_REF:0000033
ACCEPT
Summary: Phylogenetic inference of a cytokinesis role, strongly corroborated by RasG null cells becoming multinucleate in suspension.
Reason: RasG is required for normal cytokinesis; rasG-null cells fail to complete cytokinesis and become multinucleate in shaken suspension. This is a core function.
Supporting Evidence:
PMID:9245789
rasG- cells are unable to perform normal cytokinesis, becoming multinucleate when grown in suspension culture
GO:0044351 macropinocytosis
IBA
GO_REF:0000033
ACCEPT
Summary: Phylogenetic inference of a macropinocytosis role, strongly supported by genetic evidence that RasG is a major regulator of macropinocytosis.
Reason: RasG is one of the key Ras proteins driving macropinocytosis in Dictyostelium; a core function.
Supporting Evidence:
PMID:38263885
RasG is a major regulator of macropinocytosis in Dictyostelium discoideum
GO:0003924 GTPase activity
IEA
GO_REF:0000002
ACCEPT
Summary: InterPro2GO inference of GTPase activity from the Ras small-GTPase domain. Correct and core.
Reason: The Ras/P-loop GTPase domain confers intrinsic GTP hydrolysis, a core molecular function of RasG.
Supporting Evidence:
PMID:15143344
the subsequent inactivation is due to an enhancement of the intrinsic GTPase activity, which is stimulated by the GTPase-activating proteins (GAPs)
GO:0003925 G protein activity
IEA
GO_REF:0000003
ACCEPT
Summary: EC-based inference of GTP-hydrolyzing G protein activity. RasG is a monomeric guanine-nucleotide-binding signal transducer, so this MF is correct and core (GO:0003925 encompasses small monomeric GTPases).
Reason: RasG acts as a nucleotide-dependent molecular switch/signal transducer; G protein activity is a core molecular function directly demonstrated by GTP-loading (RBD pulldown) assays.
Supporting Evidence:
PMID:15143344
the Ras-binding domain (RBD) of mammalian Raf1 was capable of binding to the activated form of RasG
GO:0005525 GTP binding
IEA
GO_REF:0000002
ACCEPT
Summary: InterPro2GO inference of GTP binding from the Ras domain. Core and directly supported (GTP-bound RasG is captured by Raf1-RBD pulldowns).
Reason: RasG binds GTP/GDP through its conserved P-loop; a core molecular function.
Supporting Evidence:
PMID:15143344
the Ras-binding domain (RBD) of mammalian Raf1 was capable of binding to the activated form of RasG
GO:0005886 plasma membrane
IEA
GO_REF:0000044
ACCEPT
Summary: UniProt subcellular-location mapping to plasma membrane, consistent with the lipid-anchored, membrane-associated nature of RasG and with direct imaging.
Reason: RasG is a prenylated plasma-membrane-anchored GTPase; correct core localization.
Supporting Evidence:
PMID:15534002
GFP-RasG displayed uniform localization along the plasma membrane and cytosol
GO:0007165 signal transduction
IEA
GO_REF:0000002
KEEP AS NON CORE
Summary: Generic signal transduction inferred from the Ras domain. Correct but far less informative than the more specific small GTPase-mediated signal transduction annotation also present.
Reason: This is a high-level parent term; the specific child term GO:0007264 (small GTPase-mediated signal transduction) better captures RasG function, so this general term is retained but non-core.
Supporting Evidence:
PMID:15534002
Ras is rapidly and transiently activated in response to chemoattractant stimulation and regulates PI3K activity
GO:0016020 membrane
IEA
GO_REF:0000002
KEEP AS NON CORE
Summary: Generic membrane localization inferred from the domain. Correct but a high-level parent of the specific plasma membrane annotation.
Reason: Uninformative parent term; the specific term plasma membrane GO:0005886 is the appropriate core localization.
Supporting Evidence:
PMID:15534002
GFP-RasG displayed uniform localization along the plasma membrane and cytosol
GO:0005515 protein binding
IPI
PMID:40934557
The Ras association domain of DydA as a specific reporter of...
KEEP AS NON CORE
Summary: Captures the interaction between activated RasG and the RA1 domain of the effector DydA, used as a RasG-specific biosensor. Bare protein binding is uninformative; the biologically relevant point is effector engagement by GTP-RasG.
Reason: Documents a real RasG-effector interaction (RA1:DydA reporter) but the generic protein binding term conveys no specific function; retained as non-core.
Supporting Evidence:
PMID:40934557
RA1 preferentially binds RasG over other Ras isoforms and Rap1
GO:0019887 protein kinase regulator activity
IDA
PMID:9551080
Negative influence of RasG on chemoattractant-induced ERK2 p...
KEEP AS NON CORE
Summary: Based on the observation that constitutively activated RasG inhibits chemoattractant-induced ERK2 activating phosphorylation. This indicates RasG influences a MAP kinase, but the effect is negative and likely indirect rather than a direct kinase-regulator activity.
Reason: RasG modulates ERK2 phosphorylation, but the relationship is indirect and the more precise, directly-supported effector MF is PI3K regulation (GO:0035014). Retained as non-core.
Supporting Evidence:
PMID:9551080
Activating phosphorylation is markedly inhibited in strains overexpressing the constitutively activated RasG protein
GO:0140220 pathogen-containing vacuole
HDA
PMID:39458259
Francisella novicida-Containing Vacuole within Dictyostelium...
KEEP AS NON CORE
Summary: RasG was detected by proteomics of purified Francisella-containing vacuoles. This is an incidental high-throughput co-purification with an endomembrane compartment rather than a core RasG function; the proteome is dominated by Rab-family GTPases.
Reason: Bulk proteomic detection of a membrane-anchored GTPase on a pathogen vacuole reflects membrane trafficking during uptake, not a dedicated RasG role; retained as non-core.
Supporting Evidence:
PMID:39458259
Proteomic analyses revealed 689 proteins, including 13 small GTPases of the Rab family
GO:0019954 asexual reproduction
IMP
PMID:10906762
Mediation of cell-substratum adhesion by RasG in Dictyosteli...
KEEP AS NON CORE
Summary: RasG affects growth and phagocytosis of vegetative cells; dictyBase maps such growth/proliferation phenotypes to asexual reproduction. This is a broad developmental-cycle term rather than a specific molecular role.
Reason: The annotation reflects RasG's contribution to vegetative growth/uptake captured under a broad life-cycle term; retained as non-core.
Supporting Evidence:
PMID:10906762
RasG is crucial for Dictyostelium cell-substratum adhesion during growth and that RasG may play a role in adhesion-mediated phagocytosis
GO:0031589 cell-substrate adhesion
IMP
PMID:10906762
Mediation of cell-substratum adhesion by RasG in Dictyosteli...
ACCEPT
Summary: Expression of activated RasG(G12T) makes cells markedly more adherent to the substratum, and rasG-null cells adhere abnormally, establishing RasG as a regulator of cell-substratum adhesion.
Reason: RasG activity controls cell-substratum adhesion, a well-supported and core aspect of RasG-regulated cytoskeletal/adhesion behavior.
Supporting Evidence:
PMID:10906762
RasG is crucial for Dictyostelium cell-substratum adhesion during growth and that RasG may play a role in adhesion-mediated phagocytosis
GO:0010811 positive regulation of cell-substrate adhesion
IMP
PMID:39789437
The IQGAP-related RasGAP IqgC regulates cell-substratum adhe...
KEEP AS NON CORE
Summary: This study centers on the RasGAP IqgC and RapA in adhesion regulation. RasG's positive role in substratum adhesion is established more directly by activated-RasG experiments, so this annotation is retained but treated as a supporting, non-core adhesion role.
Reason: The cited paper primarily addresses IqgC/RapA; the positive regulation of adhesion by active RasG is supported (activated RasG increases adhesion) but the adhesion axis is one of several downstream RasG processes, retained as non-core.
Supporting Evidence:
PMID:10906762
which causes cells to become significantly more adherent to the substratum than are wild type cells
GO:1905301 regulation of macropinocytosis
IGI
PMID:38888895
Leep2A and Leep2B function as a RasGAP complex to regulate m...
ACCEPT
Summary: The Leep2A/Leep2B RasGAP complex fine-tunes Ras activity to control macropinosome formation, placing RasG within the regulatory network of macropinocytosis.
Reason: RasG activity is a central input controlling macropinocytosis; regulation of macropinocytosis is a core aspect of RasG function.
Supporting Evidence:
PMID:38888895
At the center of this signaling network are Ras GTPases, whose activation potently stimulates macropinocytosis
GO:0005515 protein binding
IPI
PMID:38888895
Leep2A and Leep2B function as a RasGAP complex to regulate m...
KEEP AS NON CORE
Summary: Captures binding between RasG and the Leep2 RasGAP complex. Bare protein binding is uninformative; the meaningful relationship is that Leep2 acts as a GAP on Ras GTPases including RasG.
Reason: Documents a real RasG-regulator (RasGAP) interaction but via an uninformative term; retained as non-core.
Supporting Evidence:
PMID:38888895
it modulates macropinosome formation by regulating the activities of three Ras family small GTPases
GO:0001891 phagocytic cup
IDA
PMID:38263885
IqgC is a potent regulator of macropinocytosis in the presen...
ACCEPT
Summary: Active RasG localizes to forming endocytic (macropinocytic/phagocytic) cups, where it recruits the RasGAP IqgC. RasG marks the cup membrane during large-scale endocytosis.
Reason: RasG is enriched at nascent endocytic cups, a core site of its action in macropinocytosis/phagocytosis.
Supporting Evidence:
PMID:38263885
interaction with RasG is indispensable for the recruitment of IqgC to forming macropinocytic cups
GO:0032880 regulation of protein localization
IMP
PMID:38263885
IqgC is a potent regulator of macropinocytosis in the presen...
ACCEPT
Summary: Recruitment/loading of the RasGAP IqgC onto macropinosomes requires RasG, so RasG controls the localization of this effector protein.
Reason: RasG governs the membrane recruitment of downstream partners (e.g. IqgC) at endocytic structures; a genuine regulatory function.
Supporting Evidence:
PMID:38263885
its loading to macropinosomes is dependent on RasG
GO:0140986 G protein-coupled chemorepellent receptor signaling pathway
IMP
PMID:34788129
A chemorepellent inhibits local Ras activation to inhibit ps...
KEEP AS NON CORE
Summary: The chemorepellent AprA locally inhibits Ras cortical activation acting through, among others, RasG, to bias cell movement away from the source. RasG participates in this chemorepulsion pathway.
Reason: RasG is a node in AprA chemorepulsion signaling, but this is a context-specific developmental/behavioral role rather than a core RasG function.
Supporting Evidence:
PMID:34788129
Ras protein RasG, protein kinase B, the p21-activated kinase PakD, and the extracellular signal-regulated kinase Erk1
GO:0140986 G protein-coupled chemorepellent receptor signaling pathway
IGI
PMID:30462573
An endogenous chemorepellent directs cell movement by inhibi...
KEEP AS NON CORE
Summary: Delineation of the AprA chemorepulsion pathway showed it uses a subset of chemoattraction components including Ras. RasG contributes to chemorepellent signaling.
Reason: Participation in AprA chemorepulsion is a specialized behavioral role, retained as non-core.
Supporting Evidence:
PMID:30462573
AprA uses a subset of chemoattraction signal transduction pathways including Ras, protein kinase A, target of rapamycin
GO:0007188 adenylate cyclase-modulating G protein-coupled receptor signaling pathway
IMP
PMID:15143344
Chemoattractant-induced Ras activation during Dictyostelium ...
KEEP AS NON CORE
Summary: During aggregation, cAMP acting via its GPCR triggers rapid, transient RasG activation. RasG is thus part of chemoattractant-GPCR signaling, though adenylyl cyclase (ACA) activation is more strongly dependent on the paralog RasC.
Reason: RasG is activated downstream of the cAMP GPCR, but the adenylate cyclase-modulating branch is predominantly a RasC function; retained as non-core for RasG.
Supporting Evidence:
PMID:15143344
RasC and RasG showed a rapid and transient activation when aggregation-competent cells were stimulated with the chemoattractant cAMP
GO:0051593 response to folic acid
IGI
PMID:23132928
Delineating the core regulatory elements crucial for directe...
ACCEPT
Summary: RasG (and RasC) are activated in response to folic acid and are required for full Ras/PI3K responses during folate-directed migration of vegetative cells.
Reason: Folate is the key vegetative chemoattractant and RasG is a core mediator of the folic-acid response; a core function.
Supporting Evidence:
PMID:23132928
Ras and phosphoinositide 3-kinase activity were significantly decreased in Ras G and Ras C/G nulls
GO:0140220 pathogen-containing vacuole
HDA
PMID:18980612
Proteome analysis of Legionella vacuoles purified by magneti...
KEEP AS NON CORE
Summary: RasG was recovered in proteomic analyses of purified Legionella- containing vacuoles, which are dominated by Arf/Rab GTPases. This is an incidental co-purification during endocytic trafficking, not a dedicated RasG role.
Reason: Bulk proteomic detection on a pathogen vacuole reflects membrane trafficking; retained as non-core.
Supporting Evidence:
PMID:18980612
revealed 566 host proteins, including known LCV components, such as the small GTPases Arf1, Rab1 and Rab7
GO:0003925 G protein activity
IDA
PMID:15352238
The identification of Dictyostelium phosphoproteins altered ...
ACCEPT
Summary: Uses the constitutively activated (GTP-locked) RasG(G12T) to probe downstream phosphorylation, consistent with RasG acting as an active G protein/signal transducer.
Reason: RasG functions as a nucleotide-dependent G protein switch; a core molecular function.
Supporting Evidence:
PMID:15352238
the effect of activated RasG, RasG(G12T), expression on the phosphorylation state of Dictyostelium proteins
GO:0035014 phosphatidylinositol 3-kinase regulator activity
IMP
PMID:23132928
Delineating the core regulatory elements crucial for directe...
ACCEPT
Summary: Loss of RasG (and RasC/G) strongly reduces PI3K activity, demonstrating that RasG is a positive regulator/activator of class I PI3K, its best-defined effector.
Reason: RasG activation of PI3K to produce PIP3 is a central, directly-supported core molecular function.
Supporting Evidence:
PMID:23132928
Ras and phosphoinositide 3-kinase activity were significantly decreased in Ras G and Ras C/G nulls
GO:0050927 positive regulation of positive chemotaxis
IMP
PMID:10725225
Functional overlap of the dictyostelium RasG, RasD and RasB ...
ACCEPT
Summary: rasG disruption reduces motility and chemotactic behavior; RasG promotes directed movement toward chemoattractants.
Reason: RasG positively promotes chemotaxis/motility, a core function.
Supporting Evidence:
PMID:10725225
a defect in cytokinesis, reduced motility and reduced growth
GO:0046587 positive regulation of calcium-dependent cell-cell adhesion
IMP
PMID:16622066
An activated Ras protein alters cell adhesion by dephosphory...
KEEP AS NON CORE
Summary: Activated RasG increases DdCAD-1-dependent cell-cell cohesion during early development by reducing DdCAD-1 phosphorylation and increasing its surface localization. This is a developmental adhesion role.
Reason: RasG modulates DdCAD-1-mediated cell-cell adhesion during early development, a specialized developmental process rather than the core RasG function.
Supporting Evidence:
PMID:16622066
cells expressing RasG(G12T) exhibited increased cell-cell cohesion, concomitant with reduced levels of DdCAD-1 phosphorylation
GO:0072697 protein localization to cell cortex
IMP
PMID:16622066
An activated Ras protein alters cell adhesion by dephosphory...
KEEP AS NON CORE
Summary: Activated RasG increases localization of the adhesion molecule DdCAD-1 at the cell surface/cortex, so RasG influences cortical protein localization in a developmental adhesion context.
Reason: This reflects RasG control of DdCAD-1 surface localization during early development, a specialized non-core role.
Supporting Evidence:
PMID:16622066
was correlated with increased localization of DdCAD-1 at the cell surface
GO:0000281 mitotic cytokinesis
IMP
PMID:10725225
Functional overlap of the dictyostelium RasG, RasD and RasB ...
ACCEPT
Summary: rasG disruption causes a cytokinesis defect, one of the principal phenotypes of rasG-null cells.
Reason: RasG is required for normal cytokinesis; a core function.
Supporting Evidence:
PMID:10725225
a defect in cytokinesis, reduced motility and reduced growth
GO:0051248 negative regulation of protein metabolic process
IDA
PMID:10725225
Functional overlap of the dictyostelium RasG, RasD and RasB ...
KEEP AS NON CORE
Summary: RasG negatively regulates the levels of the paralogous RasD (and RasB) protein in vegetative cells. This is a regulatory cross-talk between paralogs rather than a broad protein-metabolism role.
Reason: The evidence supports RasG-dependent negative control of RasD/RasB protein levels; retained under this broad term as non-core.
Supporting Evidence:
PMID:10725225
RasD protein levels are negatively regulated in vegetative cells by RasG
GO:0019887 protein kinase regulator activity
IDA
PMID:15534002
Localized Ras signaling at the leading edge regulates PI3K, ...
KEEP AS NON CORE
Summary: RasG activation stimulates PI3K and hence Akt/PKB activation. The direct effector is PI3K (a lipid kinase); regulation of the protein kinase PKB is downstream and indirect.
Reason: The precise, directly-supported effector MF is PI3K regulation (GO:0035014); the more general protein kinase regulator activity is retained as non-core.
Supporting Evidence:
PMID:15534002
chemoattractant-induced Akt/PKB activation was decreased in rasG null cells
GO:0031252 cell leading edge
IDA
PMID:15534002
Localized Ras signaling at the leading edge regulates PI3K, ...
ACCEPT
Summary: A GFP-RBD biosensor shows Ras activation localized to the leading edge of chemotaxing cells, where RasG acts to establish the front.
Reason: RasG is activated at, and acts from, the cell leading edge; a core site of action.
Supporting Evidence:
PMID:15534002
Ras activation occurs at the leading edge of chemotaxing cells
GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
IMP
PMID:15534002
Localized Ras signaling at the leading edge regulates PI3K, ...
ACCEPT
Summary: RasG activation is required for chemoattractant-induced PI3K/Akt(PKB) activation; rasG-null cells show decreased Akt/PKB activation.
Reason: Positive regulation of PI3K/PKB signaling is a core downstream output of RasG.
Supporting Evidence:
PMID:15534002
chemoattractant-induced Akt/PKB activation was decreased in rasG null cells
GO:0010629 negative regulation of gene expression
IMP
PMID:8754814
Overexpression of an activated rasG gene during growth block...
KEEP AS NON CORE
Summary: Overexpression of activated rasG-G12T during growth blocks initiation of development and represses early developmental genes (car1, pde). This is a gain-of-function developmental effect.
Reason: The effect on early gene expression reflects a developmental consequence of constitutive RasG activation rather than a core RasG function.
Supporting Evidence:
PMID:8754814
the expression of car1 and pde, genes that are normally induced soon after the initiation of development, was repressed
GO:0003925 G protein activity
IDA
PMID:17380187
Cyclic AMP signalling in Dictyostelium: G-proteins activate ...
ACCEPT
Summary: RasG is directly shown to be activated (GTP-loaded) in response to cAMP, acting as a G protein switch, with RasGEFR as its specific activator.
Reason: RasG acts as a nucleotide-dependent G protein/signal transducer; a core molecular function.
Supporting Evidence:
PMID:17380187
During Dictyostelium development, RasC and RasG are activated in response to cyclic AMP
GO:0140220 pathogen-containing vacuole
HDA
PMID:28183814
Comparative Proteomics of Purified Pathogen Vacuoles Correla...
KEEP AS NON CORE
Summary: Comparative proteomics of Legionella-containing vacuoles highlighted the small GTPase Rap1; RasG detection here is an incidental co-purification during endocytic trafficking rather than a specific RasG function.
Reason: Bulk proteomic co-purification on a pathogen vacuole; retained as non-core.
Supporting Evidence:
PMID:28183814
The small GTPase Rap1 was identified on D. discoideum LCVs containing strain Lp02 but not the
GO:0044354 macropinosome
IDA
PMID:27821733
A Diaphanous-related formin links Ras signaling directly to ...
ACCEPT
Summary: Active RasG is present on macropinosomes/endocytic cups where it directly regulates the formin ForG during large-scale endocytosis.
Reason: The macropinosome membrane is a core site of RasG action in macropinocytosis/phagocytosis.
Supporting Evidence:
PMID:27821733
ForG is directly regulated in large-scale endocytosis by RasB and RasG, which are highly related to the human proto-oncogene KRas
GO:0005515 protein binding
IPI
PMID:10473630
A novel Ras-interacting protein required for chemotaxis and ...
KEEP AS NON CORE
Summary: Captures the interaction of activated RasG with the Ras-interacting protein RIP3 (RipA), an effector required for chemotaxis and cAMP signal relay. Bare protein binding is uninformative.
Reason: Documents a real RasG-effector interaction (RIP3/RipA) but via a non-specific term; retained as non-core.
Supporting Evidence:
PMID:10473630
RIP3 preferentially interacts with an activated form of the Dictyostelium Ras protein RasG, which itself is important for cell movement
GO:0005515 protein binding
IPI
PMID:15194808
Phg2, a kinase involved in adhesion and focal site modeling ...
KEEP AS NON CORE
Summary: Relates to Phg2, an adhesion-linked serine/threonine kinase carrying a Ras-binding domain. The interaction is captured by an uninformative protein binding term.
Reason: Documents a Ras-effector (Phg2 RBD) association but via a non-specific term; retained as non-core.
Supporting Evidence:
PMID:15194808
PHG2 encodes a novel serine/threonine kinase with a ras-binding domain
GO:0005515 protein binding
IPI
PMID:20089846
A Rap/phosphatidylinositol 3-kinase pathway controls pseudop...
KEEP AS NON CORE
Summary: This study concerns a GbpD/Rap1/PI3K pathway controlling pseudopod formation and cell-substrate adhesion; the associated interaction is captured by an uninformative protein binding term.
Reason: Retained interaction annotation via a non-specific term in a Rap/PI3K adhesion context; non-core.
Supporting Evidence:
PMID:20089846
Rap1 directly binds to the Ras binding domain of PI3K
GO:0005515 protein binding
IPI
PMID:23135995
Daydreamer, a Ras effector and GSK-3 substrate, is important...
KEEP AS NON CORE
Summary: Captures the interaction with DydA (Daydreamer), an MRL-family Ras effector required for directional sensing and cell motility. Bare protein binding is uninformative.
Reason: Documents a RasG-effector interaction (DydA) but via a non-specific term; retained as non-core.
Supporting Evidence:
PMID:23135995
DydA is a putative Ras effector that is required for cell polarization and directional movement during chemotaxis
GO:0005515 protein binding
IPI
PMID:24986648
Regulation of a LATS-homolog by Ras GTPases is important for...
KEEP AS NON CORE
Summary: Captures binding of the NDR/LATS-homolog kinase NdrC to activated RasG (and RasB), an interaction important for control of cell division. Bare protein binding is uninformative.
Reason: Documents a RasG-effector interaction (NdrC) via a non-specific term; retained as non-core.
Supporting Evidence:
PMID:24986648
Further in vitro pull-down assays showed that NdrC binds RasG and RasB, and to a lesser extent RasC and Rap1
GO:0005515 protein binding
IPI
PMID:27172998
The small GTPases Ras and Rap1 bind to and control TORC2 act...
KEEP AS NON CORE
Summary: Relates to binding of Ras (and Rap1) to the TORC2 complex; in this study the strongest Ras-TOR interaction is via the paralog RasC. The generic protein binding term is uninformative.
Reason: Documents Ras-TORC2 association via a non-specific term (the study emphasizes RasC); retained as non-core.
Supporting Evidence:
PMID:27172998
Ras and Rap1 bind to and control TORC2 activity
GO:0005515 protein binding
IPI
PMID:27821733
A Diaphanous-related formin links Ras signaling directly to ...
KEEP AS NON CORE
Summary: Captures binding of activated RasG (and RasB) to the Diaphanous-related formin ForG, linking Ras signaling directly to actin assembly. Bare protein binding is uninformative.
Reason: Documents a RasG-effector interaction (ForG) via a non-specific term; retained as non-core.
Supporting Evidence:
PMID:27821733
ForG is directly regulated in large-scale endocytosis by RasB and RasG, which are highly related to the human proto-oncogene KRas
GO:0005515 protein binding
IPI
PMID:29109256
GPCR-controlled membrane recruitment of negative regulator C...
KEEP AS NON CORE
Summary: Relates to the RasGAP C2GAP1, a negative regulator of Ras signaling that is recruited to the leading edge. Bare protein binding is uninformative.
Reason: Documents a RasG-regulator (RasGAP) interaction via a non-specific term; retained as non-core.
Supporting Evidence:
PMID:29109256
C2GAP1, which localizes at the leading edge of chemotaxing cells and is activated by and essential for GPCR-mediated Ras signaling
GO:0005525 GTP binding
IDA
PMID:15143344
Chemoattractant-induced Ras activation during Dictyostelium ...
ACCEPT
Summary: Direct assay of the GTP-bound (activated) form of RasG using a Raf1-RBD pulldown demonstrates GTP binding.
Reason: GTP binding is a core molecular function directly demonstrated for RasG.
Supporting Evidence:
PMID:15143344
the Ras-binding domain (RBD) of mammalian Raf1 was capable of binding to the activated form of RasG
GO:0005811 lipid droplet
HDA
PMID:24036346
Dictyostelium lipid droplets host novel proteins.
KEEP AS NON CORE
Summary: RasG was recovered in proteomic characterization of Dictyostelium lipid droplets. This is an incidental co-purification of a membrane-anchored protein, not a dedicated lipid-droplet function.
Reason: Bulk proteomic detection on lipid droplets; retained as non-core.
Supporting Evidence:
PMID:24036346
Among the novel protein components are LdpA, a protein specific to Dictyostelium, and Net4
GO:0005938 cell cortex
IDA
PMID:24986648
Regulation of a LATS-homolog by Ras GTPases is important for...
ACCEPT
Summary: Activated RasG is a cortical/membrane-associated GTPase; the NdrC study localizes Ras activity to the cortex in the context of cell-division control.
Reason: The cell cortex is a core site of RasG activity, consistent with its membrane anchoring and leading-edge/cortical activation.
Supporting Evidence:
PMID:24986648
In cells lacking NdrC, the levels of activated RasB and RasG are up-regulated
GO:0009898 cytoplasmic side of plasma membrane
IDA
PMID:27821733
A Diaphanous-related formin links Ras signaling directly to ...
ACCEPT
Summary: RasG is prenylated and anchored to the cytoplasmic face of the plasma membrane, from which it signals to effectors such as ForG.
Reason: Consistent with the lipid-anchored orientation of RasG at the inner leaflet of the plasma membrane; a core localization.
Supporting Evidence:
PMID:27821733
ForG is directly regulated in large-scale endocytosis by RasB and RasG, which are highly related to the human proto-oncogene KRas
GO:0010856 adenylate cyclase activator activity
IGI
PMID:18180289
Rap1 activation in response to cAMP occurs downstream of ras...
KEEP AS NON CORE
Summary: In doubly-disrupted rasC/rasG cells, adenylyl cyclase (ACA) signaling is lost; however, ACA activation is predominantly a RasC-dependent process, with RasG contributing largely to the chemotactic branch.
Reason: RasG contributes to cAMP-signaling pathways, but adenylyl cyclase activation is chiefly a RasC role; retained as non-core for RasG.
Supporting Evidence:
PMID:18180289
RasG and RasC are the only two Ras subfamily proteins that directly control these pathways
GO:0019900 kinase binding
IPI
PMID:10473630
A novel Ras-interacting protein required for chemotaxis and ...
KEEP AS NON CORE
Summary: Relates to the RasG-RIP3(RipA) interaction. RIP3 is a Ras-interacting protein involved in guanylyl cyclase-linked chemotaxis signaling; the kinase binding term is only weakly informative here.
Reason: Documents a RasG partner interaction; the specific molecular meaning is better captured as effector binding, so retained as non-core.
Supporting Evidence:
PMID:10473630
RIP3 preferentially interacts with an activated form of the Dictyostelium Ras protein RasG, which itself is important for cell movement
GO:0030250 guanylate cyclase activator activity
IMP
PMID:18180289
Rap1 activation in response to cAMP occurs downstream of ras...
KEEP AS NON CORE
Summary: In vitro guanylyl cyclase activation is abolished in rasC/rasG-null cells, identifying RasG/RasC as the presumptive GTPases required, in a developmental cAMP-signaling context.
Reason: RasG contributes to guanylyl cyclase activation in the aggregation-stage cAMP pathway; a developmental-signaling role retained as non-core.
Supporting Evidence:
PMID:18180289
in vitro guanylyl cyclase activation is also abolished in the rasC
GO:0030250 guanylate cyclase activator activity
IGI
PMID:18180289
Rap1 activation in response to cAMP occurs downstream of ras...
KEEP AS NON CORE
Summary: Same finding via genetic interaction; guanylyl cyclase activation requires RasG/RasC during aggregation.
Reason: Developmental cAMP-pathway contribution; retained as non-core.
Supporting Evidence:
PMID:18180289
identifies RasG/RasC as the presumptive monomeric GTPases required for this activation
GO:0031982 vesicle
IDA
PMID:19589376
Nanovesicles released by Dictyostelium cells: a potential ca...
KEEP AS NON CORE
Summary: RasG was reported among proteins of Dictyostelium-released nanovesicles, a preparation dominated by actin and actin-related proteins. This is an incidental co-purification.
Reason: Bulk proteomic detection in released vesicles; not a core RasG function.
Supporting Evidence:
PMID:19589376
A proteomic analysis reveals a predominance of actin and actin-related proteins
GO:0043130 ubiquitin binding
IDA
PMID:24338482
Degradation of activated K-Ras orthologue via K-Ras-specific...
MARK AS OVER ANNOTATED
Summary: This study shows that activated RasG is itself targeted for degradation by polyubiquitination at K-Ras-equivalent C-terminal lysines. Being a substrate of ubiquitination is not the same as possessing a ubiquitin-binding molecular function.
Reason: The evidence demonstrates that RasG is polyubiquitinated (a substrate), which does not support a ubiquitin-binding molecular function; the term appears to over-interpret a modification event.
Supporting Evidence:
PMID:24338482
RasG, the Dictyostelium orthologue of K-Ras, is targeted for degradation by polyubiquitination
GO:0043548 phosphatidylinositol 3-kinase binding
IPI
PMID:23843627
Two distinct functions for PI3-kinases in macropinocytosis.
ACCEPT
Summary: Binding assays show RasG interacts most strongly with PI3K1/2 and PI3K4, directly engaging its principal effector, class I PI3-kinase.
Reason: Direct binding of GTP-RasG to PI3K is a core, mechanistically informative molecular function underlying macropinocytosis and chemotaxis.
Supporting Evidence:
PMID:23843627
RasG and RasS interact most strongly with PI3K1/2 and PI3K4
GO:0045335 phagocytic vesicle
HDA
PMID:16926386
Proteomics fingerprinting of phagosome maturation and eviden...
KEEP AS NON CORE
Summary: RasG was among the many signal-transduction proteins detected by proteomic fingerprinting of maturing Dictyostelium phagosomes. Consistent with a role in phagocytosis, though the detection itself is high-throughput.
Reason: Proteomic detection on phagosomes supports involvement in phagocytosis but is an incidental localization here; retained as non-core.
Supporting Evidence:
PMID:16926386
we identified 179 phagosomal proteins in the amoeba Dictyostelium, including components of signal transduction, membrane traffic, and the cytoskeleton
GO:0005886 plasma membrane
IDA
PMID:15534002
Localized Ras signaling at the leading edge regulates PI3K, ...
ACCEPT
Summary: Direct imaging shows GFP-RasG along the plasma membrane and Ras activity (GFP-RBD) at the plasma membrane/leading edge upon stimulation.
Reason: RasG acts at the plasma membrane; a core localization directly supported.
Supporting Evidence:
PMID:15534002
GFP-RasG displayed uniform localization along the plasma membrane and cytosol
GO:0044351 macropinocytosis
IMP
PMID:30967009
Function of small GTPases in Dictyostelium macropinocytosis.
ACCEPT
Summary: Genetic analysis identifies RasG (with RasS) as a key Ras protein driving macropinocytosis, which is stimulated by persistent Ras activation.
Reason: RasG is a core driver of macropinocytosis.
Supporting Evidence:
PMID:30967009
macropinocytosis is stimulated by persistent Ras activation and genetic analysis suggests that RasG and RasS are the key Ras proteins involved
GO:1901262 negative regulation of sorocarp spore cell differentiation
IMP
PMID:11222145
Expression of activated Ras during Dictyostelium development...
KEEP AS NON CORE
Summary: Developmental expression of activated rasG in prespore cells causes their transdifferentiation into prestalk cells, altering cell fate. This is a gain-of-function developmental effect.
Reason: Reflects a developmental cell-fate consequence of activated RasG rather than a core RasG molecular function; retained as non-core.
Supporting Evidence:
PMID:11222145
the expression of activated rasG in prespore cells results in their transdifferentiation into prestalk cells
GO:0006909 phagocytosis
IMP
PMID:10906762
Mediation of cell-substratum adhesion by RasG in Dictyosteli...
ACCEPT
Summary: Expression of activated RasG reduces bacterial engulfment (phagocytosis) when cells are adhered, indicating RasG regulates phagocytosis.
Reason: RasG regulates phagocytosis, a core RasG-dependent uptake process closely related to macropinocytosis.
Supporting Evidence:
PMID:10906762
engulf fewer bacteria on filter surfaces, indicating a defect in phagocytosis when cells are adhered
GO:0046847 filopodium assembly
IMP
PMID:10906762
Mediation of cell-substratum adhesion by RasG in Dictyosteli...
ACCEPT
Summary: RasG activity influences filopodial number; activated RasG dramatically reduces filopodia, and rasG-null cells show abnormal, excessive filopodia, indicating RasG regulates filopodium formation.
Reason: RasG regulates filopodium/actin-protrusion assembly, a core cytoskeletal function.
Supporting Evidence:
PMID:10906762
The expression of the activated RasG also dramatically reduces the number of filopodia on the cell surface
GO:0007015 actin filament organization
IMP
PMID:9245789
Dictyostelium RasG is required for normal motility and cytok...
ACCEPT
Summary: rasG-null cells show a wide range of actin cytoskeleton defects including loss of polarity, absence of normal lamellipodia and aberrant filopodia, establishing RasG as a regulator of actin organization.
Reason: Control of the actin cytoskeleton is a principal, core function of RasG.
Supporting Evidence:
PMID:9245789
they exhibit defective cell movement and a wide range of defects in the control of the actin cytoskeleton, including a loss of cell polarity, absence of normal lamellipodia
GO:0005515 protein binding
IPI
PMID:30622175
IQGAP-related protein IqgC suppresses Ras signaling during l...
KEEP AS NON CORE
Summary: Captures binding of the RasGAP IqgC to active RasG. Bare protein binding is uninformative; the meaningful relationship is that IqgC is a RasG-specific GAP.
Reason: Documents a RasG-regulator (RasGAP) interaction via a non-specific term; retained as non-core.
Supporting Evidence:
PMID:30622175
IqgC interacts with active RasG and exhibits RasGAP activity toward this GTPase
GO:0005515 protein binding
IPI
PMID:27009206
The novel RacE-binding protein GflB sharpens Ras activity at...
KEEP AS NON CORE
Summary: Relates to GflB, a RacE-binding protein with Ras GEF and Rho GAP domains that sharpens Ras activity at the leading edge. The interaction is captured by an uninformative protein binding term.
Reason: Documents a Ras-regulator (GflB) interaction via a non-specific term; retained as non-core.
Supporting Evidence:
PMID:27009206
GflB balances the activation of Ras and Rho GTPases, which enables cells to precisely orient signaling events
GO:1905169 regulation of protein localization to phagocytic vesicle
IMP
PMID:27821733
A Diaphanous-related formin links Ras signaling directly to ...
ACCEPT
Summary: RasG directly regulates the formin ForG at endocytic cups, controlling its recruitment/activity during phagocytosis and macropinocytosis.
Reason: RasG governs recruitment of actin-assembly machinery to phagocytic/ macropinocytic vesicles; a core function at endocytic structures.
Supporting Evidence:
PMID:27821733
ForG is directly regulated in large-scale endocytosis by RasB and RasG, which are highly related to the human proto-oncogene KRas
GO:0051591 response to cAMP
IDA
PMID:2049874
Ras-related genes in Dictyostelium discoideum.
KEEP AS NON CORE
Summary: An early characterization of Dictyostelium ras genes noting DdrasG expression in vegetative cells and early development. Support for a specific cAMP-response molecular role is limited in this reference.
Reason: RasG is activated in response to cAMP during aggregation (better established by later work); this early reference supports developmental expression, retained as non-core.
Supporting Evidence:
PMID:2049874
DdrasG is expressed in vegetative cells and during early development
GO:0019954 asexual reproduction
IGI
PMID:18180289
Rap1 activation in response to cAMP occurs downstream of ras...
KEEP AS NON CORE
Summary: RasG/RasC control cAMP signaling required for the multicellular (asexual) developmental cycle; captured under a broad life-cycle term.
Reason: Broad life-cycle term reflecting RasG's developmental-signaling contribution; retained as non-core.
Supporting Evidence:
PMID:18180289
RasG and RasC are the only two Ras subfamily proteins that directly control these pathways
GO:1903666 positive regulation of asexual reproduction
IMP
PMID:10725225
Functional overlap of the dictyostelium RasG, RasD and RasB ...
KEEP AS NON CORE
Summary: RasG supports vegetative growth and cell division underlying asexual reproduction; captured under a broad life-cycle term.
Reason: Broad life-cycle term reflecting RasG's role in growth/division; retained as non-core.
Supporting Evidence:
PMID:10725225
a defect in cytokinesis, reduced motility and reduced growth
GO:0043326 chemotaxis to folate
IMP
PMID:24742374
RasG signaling is important for optimal folate chemotaxis in...
ACCEPT
Summary: RasG is required for optimal folate chemotaxis, particularly in weak gradients, in both axenic and bacterially grown cells.
Reason: Folate chemotaxis is a core vegetative behavior of RasG.
Supporting Evidence:
PMID:24742374
Both axenic and bacterially grown cells require RasG for optimal folate chemotaxis, particularly in weak gradients
GO:0000281 mitotic cytokinesis
IMP
PMID:20833893
Ras proteins have multiple functions in vegetative cells of ...
ACCEPT
Summary: Cytokinesis is one of three distinct RasG functions in vegetative cells; RasD can fully substitute for RasG in cytokinesis but RasC cannot.
Reason: RasG is required for cytokinesis; a core function.
Supporting Evidence:
PMID:20833893
RasD is capable of totally substituting for RasG for cytokinesis and growth in suspension
GO:0043326 chemotaxis to folate
IMP
PMID:20833893
Ras proteins have multiple functions in vegetative cells of ...
ACCEPT
Summary: Folate chemotaxis is a distinct RasG function; RasC can partially, but RasD cannot, substitute for RasG in folate chemotaxis.
Reason: RasG is a core mediator of folate chemotaxis.
Supporting Evidence:
PMID:20833893
for chemotaxis to folate, RasC is capable of partially substituting for RasG, but RasD is totally without effect
GO:0044351 macropinocytosis
IMP
PMID:23843627
Two distinct functions for PI3-kinases in macropinocytosis.
ACCEPT
Summary: Single rasG mutants have severe macropinocytosis defects; RasG works with PI3K1/2 and PI3K4 to drive macropinocytosis.
Reason: RasG is a core driver of macropinocytosis through PI3K.
Supporting Evidence:
PMID:23843627
single mutants of either Ras have severe macropinocytosis defects
GO:0043327 chemotaxis to cAMP
IGI
PMID:18180289
Rap1 activation in response to cAMP occurs downstream of ras...
ACCEPT
Summary: RasG is required for cAMP chemotactic signaling during aggregation; cAMP-driven chemotaxis is abolished in rasC/rasG-null cells.
Reason: RasG is the more important Ras for cAMP chemotaxis; a core chemotactic function.
Supporting Evidence:
PMID:18180289
there was negligible signaling through both the cAMP chemotactic pathway and the adenylyl cyclase activation pathway
GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
IGI
PMID:18180289
Rap1 activation in response to cAMP occurs downstream of ras...
ACCEPT
Summary: RasG positively regulates PI3K/PKB signaling downstream of cAMP; Rap1 activation (downstream of PI3K-linked signaling) is abolished in rasG-null cells.
Reason: Positive regulation of PI3K/PKB signaling is a core downstream output of RasG.
Supporting Evidence:
PMID:18180289
Rap1 activation was totally abolished in
GO:0031152 aggregation involved in sorocarp development
IMP
PMID:16885420
Delineation of the roles played by RasG and RasC in cAMP-dep...
KEEP AS NON CORE
Summary: rasG inactivation delays aggregation and reduces early gene expression, showing RasG contributes to the aggregation stage of development.
Reason: RasG participates in developmental aggregation, a specialized developmental process rather than a core vegetative function.
Supporting Evidence:
PMID:16885420
Insertional inactivation of the rasG gene resulted in delayed aggregation and a partial inhibition of early gene expression
GO:0031152 aggregation involved in sorocarp development
IGI
PMID:16885420
Delineation of the roles played by RasG and RasC in cAMP-dep...
KEEP AS NON CORE
Summary: Comparison of rasG-, rasC- and rasC-rasG- strains shows overlapping Ras contributions to aggregation; RasG participates in the aggregation stage.
Reason: Developmental aggregation role; retained as non-core.
Supporting Evidence:
PMID:16885420
Insertional inactivation of the rasG gene resulted in delayed aggregation and a partial inhibition of early gene expression
GO:0043327 chemotaxis to cAMP
IMP
PMID:16885420
Delineation of the roles played by RasG and RasC in cAMP-dep...
ACCEPT
Summary: Signal transduction through RasG is more important than RasC for cAMP chemotaxis; chemotaxis is reduced in rasG-null cells.
Reason: RasG is a core mediator of cAMP chemotaxis.
Supporting Evidence:
PMID:16885420
signal transduction through RasG is more important in chemotaxis and early gene expression
GO:0043327 chemotaxis to cAMP
IGI
PMID:16885420
Delineation of the roles played by RasG and RasC in cAMP-dep...
ACCEPT
Summary: Genetic comparison confirms RasG is the predominant Ras for cAMP chemotaxis, with partial functional overlap with RasC.
Reason: RasG is a core mediator of cAMP chemotaxis.
Supporting Evidence:
PMID:16885420
Both chemotaxis and ACA activation were reduced in the rasG- cells, but the effect on chemotaxis was more pronounced
GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
IMP
PMID:16885420
Delineation of the roles played by RasG and RasC in cAMP-dep...
ACCEPT
Summary: RasG signaling positively contributes to the chemotactic (PI3K/PKB) arm of the cAMP response during aggregation.
Reason: Positive regulation of PI3K/PKB signaling is a core downstream output of RasG.
Supporting Evidence:
PMID:16885420
signal transduction through RasG is more important in chemotaxis and early gene expression
GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
IGI
PMID:16885420
Delineation of the roles played by RasG and RasC in cAMP-dep...
ACCEPT
Summary: Genetic interaction data support RasG positively regulating the chemotactic PI3K/PKB branch of cAMP signaling.
Reason: Positive regulation of PI3K/PKB signaling is a core downstream output of RasG.
Supporting Evidence:
PMID:16885420
Both chemotaxis and ACA activation were reduced in the rasG- cells, but the effect on chemotaxis was more pronounced
GO:0000281 mitotic cytokinesis
IMP
PMID:16822579
Cell motility and SCAR localisation in axenically growing Di...
ACCEPT
Summary: In studies of motility and SCAR localization across strains, Ras protein knockouts (including rasG) produce phenotypes during vegetative growth, consistent with the established RasG cytokinesis requirement.
Reason: RasG is required for cytokinesis (well established across multiple studies); a core function.
Supporting Evidence:
PMID:9245789
rasG- cells are unable to perform normal cytokinesis, becoming multinucleate when grown in suspension culture
GO:0000902 cell morphogenesis
IMP
PMID:16822579
Cell motility and SCAR localisation in axenically growing Di...
ACCEPT
Summary: Ras (including rasG) mutations alter cell morphology/motility during vegetative growth, consistent with RasG control of cell shape via the actin cytoskeleton.
Reason: RasG shapes cell morphology through actin/polarity control; a core function (loss of polarity and abnormal shape in rasG-null cells).
Supporting Evidence:
PMID:16822579
knockouts of members of the SCAR complex and Ras proteins, cause different phenotypes during vegetative growth in different parental strains
GO:0031589 cell-substrate adhesion
IMP
PMID:16822579
Cell motility and SCAR localisation in axenically growing Di...
ACCEPT
Summary: Consistent with RasG's established role in substratum adhesion; Ras mutants show altered vegetative-growth phenotypes including adhesion/motility behavior.
Reason: RasG regulates cell-substratum adhesion; a core function supported most directly by activated-RasG adhesion experiments.
Supporting Evidence:
PMID:10906762
which causes cells to become significantly more adherent to the substratum than are wild type cells

Core Functions

RasG is a plasma-membrane-anchored Ras small GTPase that acts as a nucleotide-dependent molecular switch. Upon chemoattractant (folate/cAMP) stimulation it is rapidly and transiently loaded with GTP at the cell cortex and leading edge, where active RasG transduces the signal to downstream effectors; its intrinsic GTPase activity (accelerated by RasGAPs such as IqgC, C2GAP1, Leep2 and NF1) resets the switch.

Supporting Evidence:
  • PMID:15534002
    Ras is rapidly and transiently activated in response to chemoattractant stimulation and regulates PI3K activity
  • PMID:15143344
    the Ras-binding domain (RBD) of mammalian Raf1 was capable of binding to the activated form of RasG

Active GTP-RasG binds and activates class I phosphatidylinositol 3-kinase (PI3K1/2, PI3K4), generating a localized PIP3 patch at the leading edge/cortex that drives F-actin-based pseudopod formation, directional sensing and PKB(Akt) activation. This RasG-PI3K axis underlies chemotaxis (to folate and cAMP), random motility, cell polarity and macropinocytosis.

Supporting Evidence:
  • PMID:23132928
    Ras and phosphoinositide 3-kinase activity were significantly decreased in Ras G and Ras C/G nulls
  • PMID:15534002
    chemoattractant-induced Akt/PKB activation was decreased in rasG null cells

RasG directly engages effectors that couple its activation to actin remodeling and bulk endocytosis, most prominently binding class I PI3-kinases and directly regulating the Diaphanous-related formin ForG at endocytic cups. Through these effectors RasG is a principal driver of macropinocytosis and phagocytosis and of the actin reorganization required for cytokinesis and cell motility.

Directly Involved In:
Supporting Evidence:
  • PMID:23843627
    RasG and RasS interact most strongly with PI3K1/2 and PI3K4
  • PMID:27821733
    ForG is directly regulated in large-scale endocytosis by RasB and RasG, which are highly related to the human proto-oncogene KRas

References

Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on Enzyme Commission mapping
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
A novel Ras-interacting protein required for chemotaxis and cyclic adenosine monophosphate signal relay in Dictyostelium.
Functional overlap of the dictyostelium RasG, RasD and RasB proteins.
Mediation of cell-substratum adhesion by RasG in Dictyostelium.
Expression of activated Ras during Dictyostelium development alters cell localization and changes cell fate.
Chemoattractant-induced Ras activation during Dictyostelium aggregation.
Phg2, a kinase involved in adhesion and focal site modeling in Dictyostelium.
The identification of Dictyostelium phosphoproteins altered in response to the activation of RasG.
Localized Ras signaling at the leading edge regulates PI3K, cell polarity, and directional cell movement.
An activated Ras protein alters cell adhesion by dephosphorylating Dictyostelium DdCAD-1.
Cell motility and SCAR localisation in axenically growing Dictyostelium cells.
Delineation of the roles played by RasG and RasC in cAMP-dependent signal transduction during the early development of Dictyostelium discoideum.
Proteomics fingerprinting of phagosome maturation and evidence for the role of a Galpha during uptake.
Cyclic AMP signalling in Dictyostelium: G-proteins activate separate Ras pathways using specific RasGEFs.
Rap1 activation in response to cAMP occurs downstream of ras activation during Dictyostelium aggregation.
Proteome analysis of Legionella vacuoles purified by magnetic immunoseparation reveals secretory and endosomal GTPases.
Nanovesicles released by Dictyostelium cells: a potential carrier for drug delivery.
A Rap/phosphatidylinositol 3-kinase pathway controls pseudopod formation [corrected].
Ras-related genes in Dictyostelium discoideum.
Ras proteins have multiple functions in vegetative cells of Dictyostelium.
Delineating the core regulatory elements crucial for directed cell migration by examining folic-acid-mediated responses.
Daydreamer, a Ras effector and GSK-3 substrate, is important for directional sensing and cell motility.
Two distinct functions for PI3-kinases in macropinocytosis.
Dictyostelium lipid droplets host novel proteins.
Degradation of activated K-Ras orthologue via K-Ras-specific lysine residues is required for cytokinesis.
RasG signaling is important for optimal folate chemotaxis in Dictyostelium.
Regulation of a LATS-homolog by Ras GTPases is important for the control of cell division.
The novel RacE-binding protein GflB sharpens Ras activity at the leading edge of migrating cells.
The small GTPases Ras and Rap1 bind to and control TORC2 activity.
A Diaphanous-related formin links Ras signaling directly to actin assembly in macropinocytosis and phagocytosis.
Comparative Proteomics of Purified Pathogen Vacuoles Correlates Intracellular Replication of Legionella pneumophila with the Small GTPase Ras-related protein 1 (Rap1).
GPCR-controlled membrane recruitment of negative regulator C2GAP1 locally inhibits Ras signaling for adaptation and long-range chemotaxis.
An endogenous chemorepellent directs cell movement by inhibiting pseudopods at one side of cells.
IQGAP-related protein IqgC suppresses Ras signaling during large-scale endocytosis.
Function of small GTPases in Dictyostelium macropinocytosis.
A chemorepellent inhibits local Ras activation to inhibit pseudopod formation to bias cell movement away from the chemorepellent.
IqgC is a potent regulator of macropinocytosis in the presence of NF1 and its loading to macropinosomes is dependent on RasG.
Leep2A and Leep2B function as a RasGAP complex to regulate macropinosome formation.
Francisella novicida-Containing Vacuole within Dictyostelium discoideum: Isolation and Proteomic Characterization.
The IQGAP-related RasGAP IqgC regulates cell-substratum adhesion in Dictyostelium discoideum.
The Ras association domain of DydA as a specific reporter of activated RasG in Dictyostelium.
Overexpression of an activated rasG gene during growth blocks the initiation of Dictyostelium development.
Dictyostelium RasG is required for normal motility and cytokinesis, but not growth.
Negative influence of RasG on chemoattractant-induced ERK2 phosphorylation in Dictyostelium.

📄 View Raw YAML

id: P15064
gene_symbol: rasG
product_type: PROTEIN
status: COMPLETE
taxon:
  id: NCBITaxon:44689
  label: Dictyostelium discoideum
description: RasG (DdrasG) is the most abundant Ras subfamily small GTPase in
  growing Dictyostelium discoideum and the closest amoebozoan relative of
  mammalian K-Ras. Like other Ras proteins it is a C-terminally prenylated,
  plasma-membrane-anchored molecular switch that cycles between an inactive
  GDP-bound and an active GTP-bound state, controlled by guanine-nucleotide
  exchange factors (RasGEFs such as GefR/Aimless) and GTPase-activating proteins
  (RasGAPs such as NF1, IqgC, C2GAP1 and the Leep2 complex). Upon chemoattractant
  (folate or cAMP) stimulation, RasG is rapidly and transiently activated at the
  leading edge and cell cortex, where GTP-loaded RasG binds and activates class I
  phosphatidylinositol 3-kinase to generate PIP3, driving F-actin-based pseudopod
  formation, directional sensing and cell motility. RasG is a principal regulator
  of chemotaxis, random motility and cell polarity, cytokinesis, macropinocytosis
  and phagocytosis, engaging effectors including PI3K, the Diaphanous-related
  formin ForG, the NDR/LATS kinase NdrC, TORC2, the Ras-interacting protein
  RIP3/RipA and the MRL-family adaptor DydA. Its functions overlap partly with the
  paralogs RasC (more specialized for cAMP relay and adenylyl cyclase activation)
  and RasD (which can substitute for RasG in cytokinesis).
existing_annotations:
- term:
    id: GO:0003924
    label: GTPase activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: Phylogenetic inference that RasG has intrinsic GTPase activity. This
      is the defining catalytic property of a Ras-family small GTPase and is
      directly supported for RasG (EC 3.6.5.2, GTP hydrolysis inactivates the
      switch).
    action: ACCEPT
    reason: RasG is a bona fide Ras GTPase that hydrolyzes GTP to GDP; the intrinsic
      GTPase activity is a core molecular function and is well conserved across the
      family.
    supported_by:
    - reference_id: PMID:15143344
      supporting_text: the subsequent inactivation is due to an enhancement of the
        intrinsic GTPase activity, which is stimulated by the GTPase-activating
        proteins (GAPs)
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: is_active_in
  review:
    summary: Phylogenetic inference of plasma membrane localization, corroborated by
      direct imaging of GFP-RasG uniformly distributed along the plasma membrane and
      activated at the cortex/leading edge.
    action: ACCEPT
    reason: RasG is prenylated and anchored to the cytoplasmic face of the plasma
      membrane, where it is activated and signals; this is a core localization.
    supported_by:
    - reference_id: PMID:15534002
      supporting_text: GFP-RasG displayed uniform localization along the plasma
        membrane and cytosol
- term:
    id: GO:0007264
    label: small GTPase-mediated signal transduction
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: Phylogenetic inference that RasG participates in small GTPase-mediated
      signal transduction. This is the core signaling role of RasG as a molecular
      switch relaying chemoattractant signals to PI3K and other effectors.
    action: ACCEPT
    reason: RasG functions as a GTP/GDP molecular switch in signal transduction, a
      core function directly demonstrated experimentally.
    supported_by:
    - reference_id: PMID:15534002
      supporting_text: Ras is rapidly and transiently activated in response to
        chemoattractant stimulation and regulates PI3K activity
- term:
    id: GO:0000281
    label: mitotic cytokinesis
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: Phylogenetic inference of a cytokinesis role, strongly corroborated by
      RasG null cells becoming multinucleate in suspension.
    action: ACCEPT
    reason: RasG is required for normal cytokinesis; rasG-null cells fail to complete
      cytokinesis and become multinucleate in shaken suspension. This is a core
      function.
    supported_by:
    - reference_id: PMID:9245789
      supporting_text: rasG- cells are unable to perform normal cytokinesis,
        becoming multinucleate when grown in suspension culture
- term:
    id: GO:0044351
    label: macropinocytosis
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: Phylogenetic inference of a macropinocytosis role, strongly supported by
      genetic evidence that RasG is a major regulator of macropinocytosis.
    action: ACCEPT
    reason: RasG is one of the key Ras proteins driving macropinocytosis in
      Dictyostelium; a core function.
    supported_by:
    - reference_id: PMID:38263885
      supporting_text: RasG is a major regulator of macropinocytosis in Dictyostelium
        discoideum
- term:
    id: GO:0003924
    label: GTPase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  review:
    summary: InterPro2GO inference of GTPase activity from the Ras small-GTPase
      domain. Correct and core.
    action: ACCEPT
    reason: The Ras/P-loop GTPase domain confers intrinsic GTP hydrolysis, a core
      molecular function of RasG.
    supported_by:
    - reference_id: PMID:15143344
      supporting_text: the subsequent inactivation is due to an enhancement of the
        intrinsic GTPase activity, which is stimulated by the GTPase-activating
        proteins (GAPs)
- term:
    id: GO:0003925
    label: G protein activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000003
  qualifier: enables
  review:
    summary: EC-based inference of GTP-hydrolyzing G protein activity. RasG is a
      monomeric guanine-nucleotide-binding signal transducer, so this MF is correct
      and core (GO:0003925 encompasses small monomeric GTPases).
    action: ACCEPT
    reason: RasG acts as a nucleotide-dependent molecular switch/signal transducer;
      G protein activity is a core molecular function directly demonstrated by
      GTP-loading (RBD pulldown) assays.
    supported_by:
    - reference_id: PMID:15143344
      supporting_text: the Ras-binding domain (RBD) of mammalian Raf1 was capable of
        binding to the activated form of RasG
- term:
    id: GO:0005525
    label: GTP binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  review:
    summary: InterPro2GO inference of GTP binding from the Ras domain. Core and
      directly supported (GTP-bound RasG is captured by Raf1-RBD pulldowns).
    action: ACCEPT
    reason: RasG binds GTP/GDP through its conserved P-loop; a core molecular
      function.
    supported_by:
    - reference_id: PMID:15143344
      supporting_text: the Ras-binding domain (RBD) of mammalian Raf1 was capable of
        binding to the activated form of RasG
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: UniProt subcellular-location mapping to plasma membrane, consistent with
      the lipid-anchored, membrane-associated nature of RasG and with direct imaging.
    action: ACCEPT
    reason: RasG is a prenylated plasma-membrane-anchored GTPase; correct core
      localization.
    supported_by:
    - reference_id: PMID:15534002
      supporting_text: GFP-RasG displayed uniform localization along the plasma
        membrane and cytosol
- term:
    id: GO:0007165
    label: signal transduction
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: Generic signal transduction inferred from the Ras domain. Correct but
      far less informative than the more specific small GTPase-mediated signal
      transduction annotation also present.
    action: KEEP_AS_NON_CORE
    reason: This is a high-level parent term; the specific child term GO:0007264
      (small GTPase-mediated signal transduction) better captures RasG function, so
      this general term is retained but non-core.
    supported_by:
    - reference_id: PMID:15534002
      supporting_text: Ras is rapidly and transiently activated in response to
        chemoattractant stimulation and regulates PI3K activity
- term:
    id: GO:0016020
    label: membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: located_in
  review:
    summary: Generic membrane localization inferred from the domain. Correct but a
      high-level parent of the specific plasma membrane annotation.
    action: KEEP_AS_NON_CORE
    reason: Uninformative parent term; the specific term plasma membrane GO:0005886
      is the appropriate core localization.
    supported_by:
    - reference_id: PMID:15534002
      supporting_text: GFP-RasG displayed uniform localization along the plasma
        membrane and cytosol
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:40934557
  qualifier: enables
  review:
    summary: Captures the interaction between activated RasG and the RA1 domain of
      the effector DydA, used as a RasG-specific biosensor. Bare protein binding is
      uninformative; the biologically relevant point is effector engagement by
      GTP-RasG.
    action: KEEP_AS_NON_CORE
    reason: Documents a real RasG-effector interaction (RA1:DydA reporter) but the
      generic protein binding term conveys no specific function; retained as
      non-core.
    supported_by:
    - reference_id: PMID:40934557
      supporting_text: RA1 preferentially binds RasG over other Ras isoforms and Rap1
- term:
    id: GO:0019887
    label: protein kinase regulator activity
  evidence_type: IDA
  original_reference_id: PMID:9551080
  qualifier: enables
  review:
    summary: Based on the observation that constitutively activated RasG inhibits
      chemoattractant-induced ERK2 activating phosphorylation. This indicates RasG
      influences a MAP kinase, but the effect is negative and likely indirect rather
      than a direct kinase-regulator activity.
    action: KEEP_AS_NON_CORE
    reason: RasG modulates ERK2 phosphorylation, but the relationship is indirect and
      the more precise, directly-supported effector MF is PI3K regulation
      (GO:0035014). Retained as non-core.
    supported_by:
    - reference_id: PMID:9551080
      supporting_text: Activating phosphorylation is markedly inhibited in strains
        overexpressing the constitutively activated RasG protein
- term:
    id: GO:0140220
    label: pathogen-containing vacuole
  evidence_type: HDA
  original_reference_id: PMID:39458259
  qualifier: located_in
  review:
    summary: RasG was detected by proteomics of purified Francisella-containing
      vacuoles. This is an incidental high-throughput co-purification with an
      endomembrane compartment rather than a core RasG function; the proteome is
      dominated by Rab-family GTPases.
    action: KEEP_AS_NON_CORE
    reason: Bulk proteomic detection of a membrane-anchored GTPase on a pathogen
      vacuole reflects membrane trafficking during uptake, not a dedicated RasG
      role; retained as non-core.
    supported_by:
    - reference_id: PMID:39458259
      supporting_text: Proteomic analyses revealed 689 proteins, including 13 small
        GTPases of the Rab family
- term:
    id: GO:0019954
    label: asexual reproduction
  evidence_type: IMP
  original_reference_id: PMID:10906762
  qualifier: acts_upstream_of_or_within
  review:
    summary: RasG affects growth and phagocytosis of vegetative cells; dictyBase maps
      such growth/proliferation phenotypes to asexual reproduction. This is a broad
      developmental-cycle term rather than a specific molecular role.
    action: KEEP_AS_NON_CORE
    reason: The annotation reflects RasG's contribution to vegetative growth/uptake
      captured under a broad life-cycle term; retained as non-core.
    supported_by:
    - reference_id: PMID:10906762
      supporting_text: RasG is crucial for Dictyostelium cell-substratum adhesion
        during growth and that RasG may play a role in adhesion-mediated phagocytosis
- term:
    id: GO:0031589
    label: cell-substrate adhesion
  evidence_type: IMP
  original_reference_id: PMID:10906762
  qualifier: acts_upstream_of_or_within
  review:
    summary: Expression of activated RasG(G12T) makes cells markedly more adherent to
      the substratum, and rasG-null cells adhere abnormally, establishing RasG as a
      regulator of cell-substratum adhesion.
    action: ACCEPT
    reason: RasG activity controls cell-substratum adhesion, a well-supported and
      core aspect of RasG-regulated cytoskeletal/adhesion behavior.
    supported_by:
    - reference_id: PMID:10906762
      supporting_text: RasG is crucial for Dictyostelium cell-substratum adhesion
        during growth and that RasG may play a role in adhesion-mediated phagocytosis
- term:
    id: GO:0010811
    label: positive regulation of cell-substrate adhesion
  evidence_type: IMP
  original_reference_id: PMID:39789437
  qualifier: acts_upstream_of_or_within
  review:
    summary: This study centers on the RasGAP IqgC and RapA in adhesion regulation.
      RasG's positive role in substratum adhesion is established more directly by
      activated-RasG experiments, so this annotation is retained but treated as a
      supporting, non-core adhesion role.
    action: KEEP_AS_NON_CORE
    reason: The cited paper primarily addresses IqgC/RapA; the positive regulation of
      adhesion by active RasG is supported (activated RasG increases adhesion) but
      the adhesion axis is one of several downstream RasG processes, retained as
      non-core.
    supported_by:
    - reference_id: PMID:10906762
      supporting_text: which causes cells to become significantly more adherent to
        the substratum than are wild type cells
- term:
    id: GO:1905301
    label: regulation of macropinocytosis
  evidence_type: IGI
  original_reference_id: PMID:38888895
  qualifier: involved_in
  review:
    summary: The Leep2A/Leep2B RasGAP complex fine-tunes Ras activity to control
      macropinosome formation, placing RasG within the regulatory network of
      macropinocytosis.
    action: ACCEPT
    reason: RasG activity is a central input controlling macropinocytosis; regulation
      of macropinocytosis is a core aspect of RasG function.
    supported_by:
    - reference_id: PMID:38888895
      supporting_text: At the center of this signaling network are Ras GTPases, whose
        activation potently stimulates macropinocytosis
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:38888895
  qualifier: enables
  review:
    summary: Captures binding between RasG and the Leep2 RasGAP complex. Bare protein
      binding is uninformative; the meaningful relationship is that Leep2 acts as a
      GAP on Ras GTPases including RasG.
    action: KEEP_AS_NON_CORE
    reason: Documents a real RasG-regulator (RasGAP) interaction but via an
      uninformative term; retained as non-core.
    supported_by:
    - reference_id: PMID:38888895
      supporting_text: it modulates macropinosome formation by regulating the
        activities of three Ras family small GTPases
- term:
    id: GO:0001891
    label: phagocytic cup
  evidence_type: IDA
  original_reference_id: PMID:38263885
  qualifier: located_in
  review:
    summary: Active RasG localizes to forming endocytic (macropinocytic/phagocytic)
      cups, where it recruits the RasGAP IqgC. RasG marks the cup membrane during
      large-scale endocytosis.
    action: ACCEPT
    reason: RasG is enriched at nascent endocytic cups, a core site of its action in
      macropinocytosis/phagocytosis.
    supported_by:
    - reference_id: PMID:38263885
      supporting_text: interaction with RasG is indispensable for the recruitment of
        IqgC to forming macropinocytic cups
- term:
    id: GO:0032880
    label: regulation of protein localization
  evidence_type: IMP
  original_reference_id: PMID:38263885
  qualifier: acts_upstream_of_or_within
  review:
    summary: Recruitment/loading of the RasGAP IqgC onto macropinosomes requires
      RasG, so RasG controls the localization of this effector protein.
    action: ACCEPT
    reason: RasG governs the membrane recruitment of downstream partners (e.g. IqgC)
      at endocytic structures; a genuine regulatory function.
    supported_by:
    - reference_id: PMID:38263885
      supporting_text: its loading to macropinosomes is dependent on RasG
- term:
    id: GO:0140986
    label: G protein-coupled chemorepellent receptor signaling pathway
  evidence_type: IMP
  original_reference_id: PMID:34788129
  qualifier: involved_in
  review:
    summary: The chemorepellent AprA locally inhibits Ras cortical activation acting
      through, among others, RasG, to bias cell movement away from the source. RasG
      participates in this chemorepulsion pathway.
    action: KEEP_AS_NON_CORE
    reason: RasG is a node in AprA chemorepulsion signaling, but this is a
      context-specific developmental/behavioral role rather than a core RasG
      function.
    supported_by:
    - reference_id: PMID:34788129
      supporting_text: Ras protein RasG, protein kinase B, the p21-activated kinase
        PakD, and the extracellular signal-regulated kinase Erk1
- term:
    id: GO:0140986
    label: G protein-coupled chemorepellent receptor signaling pathway
  evidence_type: IGI
  original_reference_id: PMID:30462573
  qualifier: acts_upstream_of_or_within
  review:
    summary: Delineation of the AprA chemorepulsion pathway showed it uses a subset
      of chemoattraction components including Ras. RasG contributes to chemorepellent
      signaling.
    action: KEEP_AS_NON_CORE
    reason: Participation in AprA chemorepulsion is a specialized behavioral role,
      retained as non-core.
    supported_by:
    - reference_id: PMID:30462573
      supporting_text: AprA uses a subset of chemoattraction signal transduction
        pathways including Ras, protein kinase A, target of rapamycin
- term:
    id: GO:0007188
    label: adenylate cyclase-modulating G protein-coupled receptor signaling pathway
  evidence_type: IMP
  original_reference_id: PMID:15143344
  qualifier: involved_in
  review:
    summary: During aggregation, cAMP acting via its GPCR triggers rapid, transient
      RasG activation. RasG is thus part of chemoattractant-GPCR signaling, though
      adenylyl cyclase (ACA) activation is more strongly dependent on the paralog
      RasC.
    action: KEEP_AS_NON_CORE
    reason: RasG is activated downstream of the cAMP GPCR, but the adenylate
      cyclase-modulating branch is predominantly a RasC function; retained as
      non-core for RasG.
    supported_by:
    - reference_id: PMID:15143344
      supporting_text: RasC and RasG showed a rapid and transient activation when
        aggregation-competent cells were stimulated with the chemoattractant cAMP
- term:
    id: GO:0051593
    label: response to folic acid
  evidence_type: IGI
  original_reference_id: PMID:23132928
  qualifier: involved_in
  review:
    summary: RasG (and RasC) are activated in response to folic acid and are required
      for full Ras/PI3K responses during folate-directed migration of vegetative
      cells.
    action: ACCEPT
    reason: Folate is the key vegetative chemoattractant and RasG is a core mediator
      of the folic-acid response; a core function.
    supported_by:
    - reference_id: PMID:23132928
      supporting_text: Ras and phosphoinositide 3-kinase activity were significantly
        decreased in Ras G and Ras C/G nulls
- term:
    id: GO:0140220
    label: pathogen-containing vacuole
  evidence_type: HDA
  original_reference_id: PMID:18980612
  qualifier: part_of
  review:
    summary: RasG was recovered in proteomic analyses of purified Legionella-
      containing vacuoles, which are dominated by Arf/Rab GTPases. This is an
      incidental co-purification during endocytic trafficking, not a dedicated RasG
      role.
    action: KEEP_AS_NON_CORE
    reason: Bulk proteomic detection on a pathogen vacuole reflects membrane
      trafficking; retained as non-core.
    supported_by:
    - reference_id: PMID:18980612
      supporting_text: revealed 566 host proteins, including known LCV components,
        such as the small GTPases Arf1, Rab1 and Rab7
- term:
    id: GO:0003925
    label: G protein activity
  evidence_type: IDA
  original_reference_id: PMID:15352238
  qualifier: enables
  review:
    summary: Uses the constitutively activated (GTP-locked) RasG(G12T) to probe
      downstream phosphorylation, consistent with RasG acting as an active G
      protein/signal transducer.
    action: ACCEPT
    reason: RasG functions as a nucleotide-dependent G protein switch; a core
      molecular function.
    supported_by:
    - reference_id: PMID:15352238
      supporting_text: the effect of activated RasG, RasG(G12T), expression on the
        phosphorylation state of Dictyostelium proteins
- term:
    id: GO:0035014
    label: phosphatidylinositol 3-kinase regulator activity
  evidence_type: IMP
  original_reference_id: PMID:23132928
  qualifier: enables
  review:
    summary: Loss of RasG (and RasC/G) strongly reduces PI3K activity, demonstrating
      that RasG is a positive regulator/activator of class I PI3K, its best-defined
      effector.
    action: ACCEPT
    reason: RasG activation of PI3K to produce PIP3 is a central, directly-supported
      core molecular function.
    supported_by:
    - reference_id: PMID:23132928
      supporting_text: Ras and phosphoinositide 3-kinase activity were significantly
        decreased in Ras G and Ras C/G nulls
- term:
    id: GO:0050927
    label: positive regulation of positive chemotaxis
  evidence_type: IMP
  original_reference_id: PMID:10725225
  qualifier: involved_in
  review:
    summary: rasG disruption reduces motility and chemotactic behavior; RasG promotes
      directed movement toward chemoattractants.
    action: ACCEPT
    reason: RasG positively promotes chemotaxis/motility, a core function.
    supported_by:
    - reference_id: PMID:10725225
      supporting_text: a defect in cytokinesis, reduced motility and reduced growth
- term:
    id: GO:0046587
    label: positive regulation of calcium-dependent cell-cell adhesion
  evidence_type: IMP
  original_reference_id: PMID:16622066
  qualifier: involved_in
  review:
    summary: Activated RasG increases DdCAD-1-dependent cell-cell cohesion during
      early development by reducing DdCAD-1 phosphorylation and increasing its
      surface localization. This is a developmental adhesion role.
    action: KEEP_AS_NON_CORE
    reason: RasG modulates DdCAD-1-mediated cell-cell adhesion during early
      development, a specialized developmental process rather than the core RasG
      function.
    supported_by:
    - reference_id: PMID:16622066
      supporting_text: cells expressing RasG(G12T) exhibited increased cell-cell
        cohesion, concomitant with reduced levels of DdCAD-1 phosphorylation
- term:
    id: GO:0072697
    label: protein localization to cell cortex
  evidence_type: IMP
  original_reference_id: PMID:16622066
  qualifier: acts_upstream_of_or_within
  review:
    summary: Activated RasG increases localization of the adhesion molecule DdCAD-1
      at the cell surface/cortex, so RasG influences cortical protein localization in
      a developmental adhesion context.
    action: KEEP_AS_NON_CORE
    reason: This reflects RasG control of DdCAD-1 surface localization during early
      development, a specialized non-core role.
    supported_by:
    - reference_id: PMID:16622066
      supporting_text: was correlated with increased localization of DdCAD-1 at the
        cell surface
- term:
    id: GO:0000281
    label: mitotic cytokinesis
  evidence_type: IMP
  original_reference_id: PMID:10725225
  qualifier: involved_in
  review:
    summary: rasG disruption causes a cytokinesis defect, one of the principal
      phenotypes of rasG-null cells.
    action: ACCEPT
    reason: RasG is required for normal cytokinesis; a core function.
    supported_by:
    - reference_id: PMID:10725225
      supporting_text: a defect in cytokinesis, reduced motility and reduced growth
- term:
    id: GO:0051248
    label: negative regulation of protein metabolic process
  evidence_type: IDA
  original_reference_id: PMID:10725225
  qualifier: involved_in
  review:
    summary: RasG negatively regulates the levels of the paralogous RasD (and RasB)
      protein in vegetative cells. This is a regulatory cross-talk between paralogs
      rather than a broad protein-metabolism role.
    action: KEEP_AS_NON_CORE
    reason: The evidence supports RasG-dependent negative control of RasD/RasB
      protein levels; retained under this broad term as non-core.
    supported_by:
    - reference_id: PMID:10725225
      supporting_text: RasD protein levels are negatively regulated in vegetative
        cells by RasG
- term:
    id: GO:0019887
    label: protein kinase regulator activity
  evidence_type: IDA
  original_reference_id: PMID:15534002
  qualifier: enables
  review:
    summary: RasG activation stimulates PI3K and hence Akt/PKB activation. The direct
      effector is PI3K (a lipid kinase); regulation of the protein kinase PKB is
      downstream and indirect.
    action: KEEP_AS_NON_CORE
    reason: The precise, directly-supported effector MF is PI3K regulation
      (GO:0035014); the more general protein kinase regulator activity is retained as
      non-core.
    supported_by:
    - reference_id: PMID:15534002
      supporting_text: chemoattractant-induced Akt/PKB activation was decreased in
        rasG null cells
- term:
    id: GO:0031252
    label: cell leading edge
  evidence_type: IDA
  original_reference_id: PMID:15534002
  qualifier: is_active_in
  review:
    summary: A GFP-RBD biosensor shows Ras activation localized to the leading edge
      of chemotaxing cells, where RasG acts to establish the front.
    action: ACCEPT
    reason: RasG is activated at, and acts from, the cell leading edge; a core site
      of action.
    supported_by:
    - reference_id: PMID:15534002
      supporting_text: Ras activation occurs at the leading edge of chemotaxing cells
- term:
    id: GO:0051897
    label: positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal
      transduction
  evidence_type: IMP
  original_reference_id: PMID:15534002
  qualifier: involved_in
  review:
    summary: RasG activation is required for chemoattractant-induced PI3K/Akt(PKB)
      activation; rasG-null cells show decreased Akt/PKB activation.
    action: ACCEPT
    reason: Positive regulation of PI3K/PKB signaling is a core downstream output of
      RasG.
    supported_by:
    - reference_id: PMID:15534002
      supporting_text: chemoattractant-induced Akt/PKB activation was decreased in
        rasG null cells
- term:
    id: GO:0010629
    label: negative regulation of gene expression
  evidence_type: IMP
  original_reference_id: PMID:8754814
  qualifier: acts_upstream_of_or_within
  review:
    summary: Overexpression of activated rasG-G12T during growth blocks initiation of
      development and represses early developmental genes (car1, pde). This is a
      gain-of-function developmental effect.
    action: KEEP_AS_NON_CORE
    reason: The effect on early gene expression reflects a developmental consequence
      of constitutive RasG activation rather than a core RasG function.
    supported_by:
    - reference_id: PMID:8754814
      supporting_text: the expression of car1 and pde, genes that are normally
        induced soon after the initiation of development, was repressed
- term:
    id: GO:0003925
    label: G protein activity
  evidence_type: IDA
  original_reference_id: PMID:17380187
  qualifier: enables
  review:
    summary: RasG is directly shown to be activated (GTP-loaded) in response to cAMP,
      acting as a G protein switch, with RasGEFR as its specific activator.
    action: ACCEPT
    reason: RasG acts as a nucleotide-dependent G protein/signal transducer; a core
      molecular function.
    supported_by:
    - reference_id: PMID:17380187
      supporting_text: During Dictyostelium development, RasC and RasG are activated
        in response to cyclic AMP
- term:
    id: GO:0140220
    label: pathogen-containing vacuole
  evidence_type: HDA
  original_reference_id: PMID:28183814
  qualifier: part_of
  review:
    summary: Comparative proteomics of Legionella-containing vacuoles highlighted the
      small GTPase Rap1; RasG detection here is an incidental co-purification during
      endocytic trafficking rather than a specific RasG function.
    action: KEEP_AS_NON_CORE
    reason: Bulk proteomic co-purification on a pathogen vacuole; retained as
      non-core.
    supported_by:
    - reference_id: PMID:28183814
      supporting_text: The small GTPase Rap1 was identified on D. discoideum LCVs
        containing strain Lp02 but not the
- term:
    id: GO:0044354
    label: macropinosome
  evidence_type: IDA
  original_reference_id: PMID:27821733
  qualifier: part_of
  review:
    summary: Active RasG is present on macropinosomes/endocytic cups where it
      directly regulates the formin ForG during large-scale endocytosis.
    action: ACCEPT
    reason: The macropinosome membrane is a core site of RasG action in
      macropinocytosis/phagocytosis.
    supported_by:
    - reference_id: PMID:27821733
      supporting_text: ForG is directly regulated in large-scale endocytosis by RasB
        and RasG, which are highly related to the human proto-oncogene KRas
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:10473630
  qualifier: enables
  review:
    summary: Captures the interaction of activated RasG with the Ras-interacting
      protein RIP3 (RipA), an effector required for chemotaxis and cAMP signal relay.
      Bare protein binding is uninformative.
    action: KEEP_AS_NON_CORE
    reason: Documents a real RasG-effector interaction (RIP3/RipA) but via a
      non-specific term; retained as non-core.
    supported_by:
    - reference_id: PMID:10473630
      supporting_text: RIP3 preferentially interacts with an activated form of the
        Dictyostelium Ras protein RasG, which itself is important for cell movement
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:15194808
  qualifier: enables
  review:
    summary: Relates to Phg2, an adhesion-linked serine/threonine kinase carrying a
      Ras-binding domain. The interaction is captured by an uninformative protein
      binding term.
    action: KEEP_AS_NON_CORE
    reason: Documents a Ras-effector (Phg2 RBD) association but via a non-specific
      term; retained as non-core.
    supported_by:
    - reference_id: PMID:15194808
      supporting_text: PHG2 encodes a novel serine/threonine kinase with a
        ras-binding domain
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:20089846
  qualifier: enables
  review:
    summary: This study concerns a GbpD/Rap1/PI3K pathway controlling pseudopod
      formation and cell-substrate adhesion; the associated interaction is captured
      by an uninformative protein binding term.
    action: KEEP_AS_NON_CORE
    reason: Retained interaction annotation via a non-specific term in a Rap/PI3K
      adhesion context; non-core.
    supported_by:
    - reference_id: PMID:20089846
      supporting_text: Rap1 directly binds to the Ras binding domain of PI3K
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:23135995
  qualifier: enables
  review:
    summary: Captures the interaction with DydA (Daydreamer), an MRL-family Ras
      effector required for directional sensing and cell motility. Bare protein
      binding is uninformative.
    action: KEEP_AS_NON_CORE
    reason: Documents a RasG-effector interaction (DydA) but via a non-specific term;
      retained as non-core.
    supported_by:
    - reference_id: PMID:23135995
      supporting_text: DydA is a putative Ras effector that is required for cell
        polarization and directional movement during chemotaxis
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:24986648
  qualifier: enables
  review:
    summary: Captures binding of the NDR/LATS-homolog kinase NdrC to activated RasG
      (and RasB), an interaction important for control of cell division. Bare protein
      binding is uninformative.
    action: KEEP_AS_NON_CORE
    reason: Documents a RasG-effector interaction (NdrC) via a non-specific term;
      retained as non-core.
    supported_by:
    - reference_id: PMID:24986648
      supporting_text: Further in vitro pull-down assays showed that NdrC binds RasG
        and RasB, and to a lesser extent RasC and Rap1
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:27172998
  qualifier: enables
  review:
    summary: Relates to binding of Ras (and Rap1) to the TORC2 complex; in this study
      the strongest Ras-TOR interaction is via the paralog RasC. The generic protein
      binding term is uninformative.
    action: KEEP_AS_NON_CORE
    reason: Documents Ras-TORC2 association via a non-specific term (the study
      emphasizes RasC); retained as non-core.
    supported_by:
    - reference_id: PMID:27172998
      supporting_text: Ras and Rap1 bind to and control TORC2 activity
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:27821733
  qualifier: enables
  review:
    summary: Captures binding of activated RasG (and RasB) to the Diaphanous-related
      formin ForG, linking Ras signaling directly to actin assembly. Bare protein
      binding is uninformative.
    action: KEEP_AS_NON_CORE
    reason: Documents a RasG-effector interaction (ForG) via a non-specific term;
      retained as non-core.
    supported_by:
    - reference_id: PMID:27821733
      supporting_text: ForG is directly regulated in large-scale endocytosis by RasB
        and RasG, which are highly related to the human proto-oncogene KRas
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:29109256
  qualifier: enables
  review:
    summary: Relates to the RasGAP C2GAP1, a negative regulator of Ras signaling that
      is recruited to the leading edge. Bare protein binding is uninformative.
    action: KEEP_AS_NON_CORE
    reason: Documents a RasG-regulator (RasGAP) interaction via a non-specific term;
      retained as non-core.
    supported_by:
    - reference_id: PMID:29109256
      supporting_text: C2GAP1, which localizes at the leading edge of chemotaxing
        cells and is activated by and essential for GPCR-mediated Ras signaling
- term:
    id: GO:0005525
    label: GTP binding
  evidence_type: IDA
  original_reference_id: PMID:15143344
  qualifier: enables
  review:
    summary: Direct assay of the GTP-bound (activated) form of RasG using a Raf1-RBD
      pulldown demonstrates GTP binding.
    action: ACCEPT
    reason: GTP binding is a core molecular function directly demonstrated for RasG.
    supported_by:
    - reference_id: PMID:15143344
      supporting_text: the Ras-binding domain (RBD) of mammalian Raf1 was capable of
        binding to the activated form of RasG
- term:
    id: GO:0005811
    label: lipid droplet
  evidence_type: HDA
  original_reference_id: PMID:24036346
  qualifier: part_of
  review:
    summary: RasG was recovered in proteomic characterization of Dictyostelium lipid
      droplets. This is an incidental co-purification of a membrane-anchored protein,
      not a dedicated lipid-droplet function.
    action: KEEP_AS_NON_CORE
    reason: Bulk proteomic detection on lipid droplets; retained as non-core.
    supported_by:
    - reference_id: PMID:24036346
      supporting_text: Among the novel protein components are LdpA, a protein
        specific to Dictyostelium, and Net4
- term:
    id: GO:0005938
    label: cell cortex
  evidence_type: IDA
  original_reference_id: PMID:24986648
  qualifier: part_of
  review:
    summary: Activated RasG is a cortical/membrane-associated GTPase; the NdrC study
      localizes Ras activity to the cortex in the context of cell-division control.
    action: ACCEPT
    reason: The cell cortex is a core site of RasG activity, consistent with its
      membrane anchoring and leading-edge/cortical activation.
    supported_by:
    - reference_id: PMID:24986648
      supporting_text: In cells lacking NdrC, the levels of activated RasB and RasG
        are up-regulated
- term:
    id: GO:0009898
    label: cytoplasmic side of plasma membrane
  evidence_type: IDA
  original_reference_id: PMID:27821733
  qualifier: is_active_in
  review:
    summary: RasG is prenylated and anchored to the cytoplasmic face of the plasma
      membrane, from which it signals to effectors such as ForG.
    action: ACCEPT
    reason: Consistent with the lipid-anchored orientation of RasG at the inner
      leaflet of the plasma membrane; a core localization.
    supported_by:
    - reference_id: PMID:27821733
      supporting_text: ForG is directly regulated in large-scale endocytosis by RasB
        and RasG, which are highly related to the human proto-oncogene KRas
- term:
    id: GO:0010856
    label: adenylate cyclase activator activity
  evidence_type: IGI
  original_reference_id: PMID:18180289
  qualifier: enables
  review:
    summary: In doubly-disrupted rasC/rasG cells, adenylyl cyclase (ACA) signaling is
      lost; however, ACA activation is predominantly a RasC-dependent process, with
      RasG contributing largely to the chemotactic branch.
    action: KEEP_AS_NON_CORE
    reason: RasG contributes to cAMP-signaling pathways, but adenylyl cyclase
      activation is chiefly a RasC role; retained as non-core for RasG.
    supported_by:
    - reference_id: PMID:18180289
      supporting_text: RasG and RasC are the only two Ras subfamily proteins that
        directly control these pathways
- term:
    id: GO:0019900
    label: kinase binding
  evidence_type: IPI
  original_reference_id: PMID:10473630
  qualifier: enables
  review:
    summary: Relates to the RasG-RIP3(RipA) interaction. RIP3 is a Ras-interacting
      protein involved in guanylyl cyclase-linked chemotaxis signaling; the kinase
      binding term is only weakly informative here.
    action: KEEP_AS_NON_CORE
    reason: Documents a RasG partner interaction; the specific molecular meaning is
      better captured as effector binding, so retained as non-core.
    supported_by:
    - reference_id: PMID:10473630
      supporting_text: RIP3 preferentially interacts with an activated form of the
        Dictyostelium Ras protein RasG, which itself is important for cell movement
- term:
    id: GO:0030250
    label: guanylate cyclase activator activity
  evidence_type: IMP
  original_reference_id: PMID:18180289
  qualifier: enables
  review:
    summary: In vitro guanylyl cyclase activation is abolished in rasC/rasG-null
      cells, identifying RasG/RasC as the presumptive GTPases required, in a
      developmental cAMP-signaling context.
    action: KEEP_AS_NON_CORE
    reason: RasG contributes to guanylyl cyclase activation in the aggregation-stage
      cAMP pathway; a developmental-signaling role retained as non-core.
    supported_by:
    - reference_id: PMID:18180289
      supporting_text: in vitro guanylyl cyclase activation is also abolished in the
        rasC
- term:
    id: GO:0030250
    label: guanylate cyclase activator activity
  evidence_type: IGI
  original_reference_id: PMID:18180289
  qualifier: enables
  review:
    summary: Same finding via genetic interaction; guanylyl cyclase activation
      requires RasG/RasC during aggregation.
    action: KEEP_AS_NON_CORE
    reason: Developmental cAMP-pathway contribution; retained as non-core.
    supported_by:
    - reference_id: PMID:18180289
      supporting_text: identifies RasG/RasC as the presumptive monomeric GTPases
        required for this activation
- term:
    id: GO:0031982
    label: vesicle
  evidence_type: IDA
  original_reference_id: PMID:19589376
  qualifier: part_of
  review:
    summary: RasG was reported among proteins of Dictyostelium-released nanovesicles,
      a preparation dominated by actin and actin-related proteins. This is an
      incidental co-purification.
    action: KEEP_AS_NON_CORE
    reason: Bulk proteomic detection in released vesicles; not a core RasG function.
    supported_by:
    - reference_id: PMID:19589376
      supporting_text: A proteomic analysis reveals a predominance of actin and
        actin-related proteins
- term:
    id: GO:0043130
    label: ubiquitin binding
  evidence_type: IDA
  original_reference_id: PMID:24338482
  qualifier: enables
  review:
    summary: This study shows that activated RasG is itself targeted for degradation
      by polyubiquitination at K-Ras-equivalent C-terminal lysines. Being a substrate
      of ubiquitination is not the same as possessing a ubiquitin-binding molecular
      function.
    action: MARK_AS_OVER_ANNOTATED
    reason: The evidence demonstrates that RasG is polyubiquitinated (a substrate),
      which does not support a ubiquitin-binding molecular function; the term appears
      to over-interpret a modification event.
    supported_by:
    - reference_id: PMID:24338482
      supporting_text: RasG, the Dictyostelium orthologue of K-Ras, is targeted for
        degradation by polyubiquitination
- term:
    id: GO:0043548
    label: phosphatidylinositol 3-kinase binding
  evidence_type: IPI
  original_reference_id: PMID:23843627
  qualifier: enables
  review:
    summary: Binding assays show RasG interacts most strongly with PI3K1/2 and PI3K4,
      directly engaging its principal effector, class I PI3-kinase.
    action: ACCEPT
    reason: Direct binding of GTP-RasG to PI3K is a core, mechanistically informative
      molecular function underlying macropinocytosis and chemotaxis.
    supported_by:
    - reference_id: PMID:23843627
      supporting_text: RasG and RasS interact most strongly with PI3K1/2 and PI3K4
- term:
    id: GO:0045335
    label: phagocytic vesicle
  evidence_type: HDA
  original_reference_id: PMID:16926386
  qualifier: part_of
  review:
    summary: RasG was among the many signal-transduction proteins detected by
      proteomic fingerprinting of maturing Dictyostelium phagosomes. Consistent with
      a role in phagocytosis, though the detection itself is high-throughput.
    action: KEEP_AS_NON_CORE
    reason: Proteomic detection on phagosomes supports involvement in phagocytosis
      but is an incidental localization here; retained as non-core.
    supported_by:
    - reference_id: PMID:16926386
      supporting_text: we identified 179 phagosomal proteins in the amoeba
        Dictyostelium, including components of signal transduction, membrane traffic,
        and the cytoskeleton
- term:
    id: GO:0005886
    label: plasma membrane
  evidence_type: IDA
  original_reference_id: PMID:15534002
  qualifier: is_active_in
  review:
    summary: Direct imaging shows GFP-RasG along the plasma membrane and Ras activity
      (GFP-RBD) at the plasma membrane/leading edge upon stimulation.
    action: ACCEPT
    reason: RasG acts at the plasma membrane; a core localization directly supported.
    supported_by:
    - reference_id: PMID:15534002
      supporting_text: GFP-RasG displayed uniform localization along the plasma
        membrane and cytosol
- term:
    id: GO:0044351
    label: macropinocytosis
  evidence_type: IMP
  original_reference_id: PMID:30967009
  qualifier: acts_upstream_of_or_within
  review:
    summary: Genetic analysis identifies RasG (with RasS) as a key Ras protein
      driving macropinocytosis, which is stimulated by persistent Ras activation.
    action: ACCEPT
    reason: RasG is a core driver of macropinocytosis.
    supported_by:
    - reference_id: PMID:30967009
      supporting_text: macropinocytosis is stimulated by persistent Ras activation and
        genetic analysis suggests that RasG and RasS are the key Ras proteins involved
- term:
    id: GO:1901262
    label: negative regulation of sorocarp spore cell differentiation
  evidence_type: IMP
  original_reference_id: PMID:11222145
  qualifier: acts_upstream_of_or_within
  review:
    summary: Developmental expression of activated rasG in prespore cells causes their
      transdifferentiation into prestalk cells, altering cell fate. This is a
      gain-of-function developmental effect.
    action: KEEP_AS_NON_CORE
    reason: Reflects a developmental cell-fate consequence of activated RasG rather
      than a core RasG molecular function; retained as non-core.
    supported_by:
    - reference_id: PMID:11222145
      supporting_text: the expression of activated rasG in prespore cells results in
        their transdifferentiation into prestalk cells
- term:
    id: GO:0006909
    label: phagocytosis
  evidence_type: IMP
  original_reference_id: PMID:10906762
  qualifier: acts_upstream_of_or_within
  review:
    summary: Expression of activated RasG reduces bacterial engulfment (phagocytosis)
      when cells are adhered, indicating RasG regulates phagocytosis.
    action: ACCEPT
    reason: RasG regulates phagocytosis, a core RasG-dependent uptake process closely
      related to macropinocytosis.
    supported_by:
    - reference_id: PMID:10906762
      supporting_text: engulf fewer bacteria on filter surfaces, indicating a defect
        in phagocytosis when cells are adhered
- term:
    id: GO:0046847
    label: filopodium assembly
  evidence_type: IMP
  original_reference_id: PMID:10906762
  qualifier: acts_upstream_of_or_within
  review:
    summary: RasG activity influences filopodial number; activated RasG dramatically
      reduces filopodia, and rasG-null cells show abnormal, excessive filopodia,
      indicating RasG regulates filopodium formation.
    action: ACCEPT
    reason: RasG regulates filopodium/actin-protrusion assembly, a core cytoskeletal
      function.
    supported_by:
    - reference_id: PMID:10906762
      supporting_text: The expression of the activated RasG also dramatically reduces
        the number of filopodia on the cell surface
- term:
    id: GO:0007015
    label: actin filament organization
  evidence_type: IMP
  original_reference_id: PMID:9245789
  qualifier: acts_upstream_of_or_within
  review:
    summary: rasG-null cells show a wide range of actin cytoskeleton defects including
      loss of polarity, absence of normal lamellipodia and aberrant filopodia,
      establishing RasG as a regulator of actin organization.
    action: ACCEPT
    reason: Control of the actin cytoskeleton is a principal, core function of RasG.
    supported_by:
    - reference_id: PMID:9245789
      supporting_text: they exhibit defective cell movement and a wide range of
        defects in the control of the actin cytoskeleton, including a loss of cell
        polarity, absence of normal lamellipodia
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:30622175
  qualifier: enables
  review:
    summary: Captures binding of the RasGAP IqgC to active RasG. Bare protein binding
      is uninformative; the meaningful relationship is that IqgC is a RasG-specific
      GAP.
    action: KEEP_AS_NON_CORE
    reason: Documents a RasG-regulator (RasGAP) interaction via a non-specific term;
      retained as non-core.
    supported_by:
    - reference_id: PMID:30622175
      supporting_text: IqgC interacts with active RasG and exhibits RasGAP activity
        toward this GTPase
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:27009206
  qualifier: enables
  review:
    summary: Relates to GflB, a RacE-binding protein with Ras GEF and Rho GAP domains
      that sharpens Ras activity at the leading edge. The interaction is captured by
      an uninformative protein binding term.
    action: KEEP_AS_NON_CORE
    reason: Documents a Ras-regulator (GflB) interaction via a non-specific term;
      retained as non-core.
    supported_by:
    - reference_id: PMID:27009206
      supporting_text: GflB balances the activation of Ras and Rho GTPases, which
        enables cells to precisely orient signaling events
- term:
    id: GO:1905169
    label: regulation of protein localization to phagocytic vesicle
  evidence_type: IMP
  original_reference_id: PMID:27821733
  qualifier: acts_upstream_of_or_within
  review:
    summary: RasG directly regulates the formin ForG at endocytic cups, controlling
      its recruitment/activity during phagocytosis and macropinocytosis.
    action: ACCEPT
    reason: RasG governs recruitment of actin-assembly machinery to phagocytic/
      macropinocytic vesicles; a core function at endocytic structures.
    supported_by:
    - reference_id: PMID:27821733
      supporting_text: ForG is directly regulated in large-scale endocytosis by RasB
        and RasG, which are highly related to the human proto-oncogene KRas
- term:
    id: GO:0051591
    label: response to cAMP
  evidence_type: IDA
  original_reference_id: PMID:2049874
  qualifier: involved_in
  review:
    summary: An early characterization of Dictyostelium ras genes noting DdrasG
      expression in vegetative cells and early development. Support for a specific
      cAMP-response molecular role is limited in this reference.
    action: KEEP_AS_NON_CORE
    reason: RasG is activated in response to cAMP during aggregation (better
      established by later work); this early reference supports developmental
      expression, retained as non-core.
    supported_by:
    - reference_id: PMID:2049874
      supporting_text: DdrasG is expressed in vegetative cells and during early
        development
- term:
    id: GO:0019954
    label: asexual reproduction
  evidence_type: IGI
  original_reference_id: PMID:18180289
  qualifier: acts_upstream_of_or_within
  review:
    summary: RasG/RasC control cAMP signaling required for the multicellular (asexual)
      developmental cycle; captured under a broad life-cycle term.
    action: KEEP_AS_NON_CORE
    reason: Broad life-cycle term reflecting RasG's developmental-signaling
      contribution; retained as non-core.
    supported_by:
    - reference_id: PMID:18180289
      supporting_text: RasG and RasC are the only two Ras subfamily proteins that
        directly control these pathways
- term:
    id: GO:1903666
    label: positive regulation of asexual reproduction
  evidence_type: IMP
  original_reference_id: PMID:10725225
  qualifier: acts_upstream_of_or_within
  review:
    summary: RasG supports vegetative growth and cell division underlying asexual
      reproduction; captured under a broad life-cycle term.
    action: KEEP_AS_NON_CORE
    reason: Broad life-cycle term reflecting RasG's role in growth/division; retained
      as non-core.
    supported_by:
    - reference_id: PMID:10725225
      supporting_text: a defect in cytokinesis, reduced motility and reduced growth
- term:
    id: GO:0043326
    label: chemotaxis to folate
  evidence_type: IMP
  original_reference_id: PMID:24742374
  qualifier: acts_upstream_of_or_within
  review:
    summary: RasG is required for optimal folate chemotaxis, particularly in weak
      gradients, in both axenic and bacterially grown cells.
    action: ACCEPT
    reason: Folate chemotaxis is a core vegetative behavior of RasG.
    supported_by:
    - reference_id: PMID:24742374
      supporting_text: Both axenic and bacterially grown cells require RasG for
        optimal folate chemotaxis, particularly in weak gradients
- term:
    id: GO:0000281
    label: mitotic cytokinesis
  evidence_type: IMP
  original_reference_id: PMID:20833893
  qualifier: acts_upstream_of_or_within
  review:
    summary: Cytokinesis is one of three distinct RasG functions in vegetative cells;
      RasD can fully substitute for RasG in cytokinesis but RasC cannot.
    action: ACCEPT
    reason: RasG is required for cytokinesis; a core function.
    supported_by:
    - reference_id: PMID:20833893
      supporting_text: RasD is capable of totally substituting for RasG for
        cytokinesis and growth in suspension
- term:
    id: GO:0043326
    label: chemotaxis to folate
  evidence_type: IMP
  original_reference_id: PMID:20833893
  qualifier: acts_upstream_of_or_within
  review:
    summary: Folate chemotaxis is a distinct RasG function; RasC can partially, but
      RasD cannot, substitute for RasG in folate chemotaxis.
    action: ACCEPT
    reason: RasG is a core mediator of folate chemotaxis.
    supported_by:
    - reference_id: PMID:20833893
      supporting_text: for chemotaxis to folate, RasC is capable of partially
        substituting for RasG, but RasD is totally without effect
- term:
    id: GO:0044351
    label: macropinocytosis
  evidence_type: IMP
  original_reference_id: PMID:23843627
  qualifier: acts_upstream_of_or_within
  review:
    summary: Single rasG mutants have severe macropinocytosis defects; RasG works
      with PI3K1/2 and PI3K4 to drive macropinocytosis.
    action: ACCEPT
    reason: RasG is a core driver of macropinocytosis through PI3K.
    supported_by:
    - reference_id: PMID:23843627
      supporting_text: single mutants of either Ras have severe macropinocytosis
        defects
- term:
    id: GO:0043327
    label: chemotaxis to cAMP
  evidence_type: IGI
  original_reference_id: PMID:18180289
  qualifier: acts_upstream_of_or_within
  review:
    summary: RasG is required for cAMP chemotactic signaling during aggregation;
      cAMP-driven chemotaxis is abolished in rasC/rasG-null cells.
    action: ACCEPT
    reason: RasG is the more important Ras for cAMP chemotaxis; a core chemotactic
      function.
    supported_by:
    - reference_id: PMID:18180289
      supporting_text: there was negligible signaling through both the cAMP
        chemotactic pathway and the adenylyl cyclase activation pathway
- term:
    id: GO:0051897
    label: positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal
      transduction
  evidence_type: IGI
  original_reference_id: PMID:18180289
  qualifier: acts_upstream_of_or_within
  review:
    summary: RasG positively regulates PI3K/PKB signaling downstream of cAMP; Rap1
      activation (downstream of PI3K-linked signaling) is abolished in rasG-null
      cells.
    action: ACCEPT
    reason: Positive regulation of PI3K/PKB signaling is a core downstream output of
      RasG.
    supported_by:
    - reference_id: PMID:18180289
      supporting_text: Rap1 activation was totally abolished in
- term:
    id: GO:0031152
    label: aggregation involved in sorocarp development
  evidence_type: IMP
  original_reference_id: PMID:16885420
  qualifier: acts_upstream_of_or_within
  review:
    summary: rasG inactivation delays aggregation and reduces early gene expression,
      showing RasG contributes to the aggregation stage of development.
    action: KEEP_AS_NON_CORE
    reason: RasG participates in developmental aggregation, a specialized
      developmental process rather than a core vegetative function.
    supported_by:
    - reference_id: PMID:16885420
      supporting_text: Insertional inactivation of the rasG gene resulted in delayed
        aggregation and a partial inhibition of early gene expression
- term:
    id: GO:0031152
    label: aggregation involved in sorocarp development
  evidence_type: IGI
  original_reference_id: PMID:16885420
  qualifier: acts_upstream_of_or_within
  review:
    summary: Comparison of rasG-, rasC- and rasC-rasG- strains shows overlapping Ras
      contributions to aggregation; RasG participates in the aggregation stage.
    action: KEEP_AS_NON_CORE
    reason: Developmental aggregation role; retained as non-core.
    supported_by:
    - reference_id: PMID:16885420
      supporting_text: Insertional inactivation of the rasG gene resulted in delayed
        aggregation and a partial inhibition of early gene expression
- term:
    id: GO:0043327
    label: chemotaxis to cAMP
  evidence_type: IMP
  original_reference_id: PMID:16885420
  qualifier: acts_upstream_of_or_within
  review:
    summary: Signal transduction through RasG is more important than RasC for cAMP
      chemotaxis; chemotaxis is reduced in rasG-null cells.
    action: ACCEPT
    reason: RasG is a core mediator of cAMP chemotaxis.
    supported_by:
    - reference_id: PMID:16885420
      supporting_text: signal transduction through RasG is more important in
        chemotaxis and early gene expression
- term:
    id: GO:0043327
    label: chemotaxis to cAMP
  evidence_type: IGI
  original_reference_id: PMID:16885420
  qualifier: acts_upstream_of_or_within
  review:
    summary: Genetic comparison confirms RasG is the predominant Ras for cAMP
      chemotaxis, with partial functional overlap with RasC.
    action: ACCEPT
    reason: RasG is a core mediator of cAMP chemotaxis.
    supported_by:
    - reference_id: PMID:16885420
      supporting_text: Both chemotaxis and ACA activation were reduced in the rasG-
        cells, but the effect on chemotaxis was more pronounced
- term:
    id: GO:0051897
    label: positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal
      transduction
  evidence_type: IMP
  original_reference_id: PMID:16885420
  qualifier: acts_upstream_of_or_within
  review:
    summary: RasG signaling positively contributes to the chemotactic (PI3K/PKB) arm
      of the cAMP response during aggregation.
    action: ACCEPT
    reason: Positive regulation of PI3K/PKB signaling is a core downstream output of
      RasG.
    supported_by:
    - reference_id: PMID:16885420
      supporting_text: signal transduction through RasG is more important in
        chemotaxis and early gene expression
- term:
    id: GO:0051897
    label: positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal
      transduction
  evidence_type: IGI
  original_reference_id: PMID:16885420
  qualifier: acts_upstream_of_or_within
  review:
    summary: Genetic interaction data support RasG positively regulating the
      chemotactic PI3K/PKB branch of cAMP signaling.
    action: ACCEPT
    reason: Positive regulation of PI3K/PKB signaling is a core downstream output of
      RasG.
    supported_by:
    - reference_id: PMID:16885420
      supporting_text: Both chemotaxis and ACA activation were reduced in the rasG-
        cells, but the effect on chemotaxis was more pronounced
- term:
    id: GO:0000281
    label: mitotic cytokinesis
  evidence_type: IMP
  original_reference_id: PMID:16822579
  qualifier: acts_upstream_of_or_within
  review:
    summary: In studies of motility and SCAR localization across strains, Ras protein
      knockouts (including rasG) produce phenotypes during vegetative growth,
      consistent with the established RasG cytokinesis requirement.
    action: ACCEPT
    reason: RasG is required for cytokinesis (well established across multiple
      studies); a core function.
    supported_by:
    - reference_id: PMID:9245789
      supporting_text: rasG- cells are unable to perform normal cytokinesis,
        becoming multinucleate when grown in suspension culture
- term:
    id: GO:0000902
    label: cell morphogenesis
  evidence_type: IMP
  original_reference_id: PMID:16822579
  qualifier: acts_upstream_of_or_within
  review:
    summary: Ras (including rasG) mutations alter cell morphology/motility during
      vegetative growth, consistent with RasG control of cell shape via the actin
      cytoskeleton.
    action: ACCEPT
    reason: RasG shapes cell morphology through actin/polarity control; a core
      function (loss of polarity and abnormal shape in rasG-null cells).
    supported_by:
    - reference_id: PMID:16822579
      supporting_text: knockouts of members of the SCAR complex and Ras proteins,
        cause different phenotypes during vegetative growth in different parental
        strains
- term:
    id: GO:0031589
    label: cell-substrate adhesion
  evidence_type: IMP
  original_reference_id: PMID:16822579
  qualifier: acts_upstream_of_or_within
  review:
    summary: Consistent with RasG's established role in substratum adhesion; Ras
      mutants show altered vegetative-growth phenotypes including adhesion/motility
      behavior.
    action: ACCEPT
    reason: RasG regulates cell-substratum adhesion; a core function supported most
      directly by activated-RasG adhesion experiments.
    supported_by:
    - reference_id: PMID:10906762
      supporting_text: which causes cells to become significantly more adherent to
        the substratum than are wild type cells
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO
    terms
  findings: []
- id: GO_REF:0000003
  title: Gene Ontology annotation based on Enzyme Commission mapping
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location
    vocabulary mapping, accompanied by conservative changes to GO terms applied by
    UniProt
  findings: []
- id: PMID:10473630
  title: A novel Ras-interacting protein required for chemotaxis and cyclic adenosine
    monophosphate signal relay in Dictyostelium.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: PubMed-verified; RIP3/RipA preferentially binds activated RasG and
      links chemotaxis and cAMP signal relay.
- id: PMID:10725225
  title: Functional overlap of the dictyostelium RasG, RasD and RasB proteins.
  findings: []
- id: PMID:10906762
  title: Mediation of cell-substratum adhesion by RasG in Dictyostelium.
  findings: []
- id: PMID:11222145
  title: Expression of activated Ras during Dictyostelium development alters cell
    localization and changes cell fate.
  findings: []
- id: PMID:15143344
  title: Chemoattractant-induced Ras activation during Dictyostelium aggregation.
  findings: []
- id: PMID:15194808
  title: Phg2, a kinase involved in adhesion and focal site modeling in Dictyostelium.
  findings: []
- id: PMID:15352238
  title: The identification of Dictyostelium phosphoproteins altered in response to
    the activation of RasG.
  findings: []
- id: PMID:15534002
  title: Localized Ras signaling at the leading edge regulates PI3K, cell polarity,
    and directional cell movement.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: PubMed-verified full text; establishes leading-edge RasG activation
      driving PI3K and directional movement (GFP-RasG plasma membrane localization,
      reduced Akt/PKB in rasG null).
- id: PMID:16622066
  title: An activated Ras protein alters cell adhesion by dephosphorylating Dictyostelium
    DdCAD-1.
  findings: []
- id: PMID:16822579
  title: Cell motility and SCAR localisation in axenically growing Dictyostelium cells.
  findings: []
- id: PMID:16885420
  title: Delineation of the roles played by RasG and RasC in cAMP-dependent signal
    transduction during the early development of Dictyostelium discoideum.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: PubMed-verified; RasG is more important for cAMP chemotaxis and
      early gene expression while RasC is more important for adenylyl cyclase
      activation.
- id: PMID:16926386
  title: Proteomics fingerprinting of phagosome maturation and evidence for the role
    of a Galpha during uptake.
  findings: []
- id: PMID:17380187
  title: 'Cyclic AMP signalling in Dictyostelium: G-proteins activate separate Ras
    pathways using specific RasGEFs.'
  findings: []
- id: PMID:18180289
  title: Rap1 activation in response to cAMP occurs downstream of ras activation during
    Dictyostelium aggregation.
  findings: []
- id: PMID:18980612
  title: Proteome analysis of Legionella vacuoles purified by magnetic immunoseparation
    reveals secretory and endosomal GTPases.
  findings: []
- id: PMID:19589376
  title: 'Nanovesicles released by Dictyostelium cells: a potential carrier for drug
    delivery.'
  findings: []
- id: PMID:20089846
  title: A Rap/phosphatidylinositol 3-kinase pathway controls pseudopod formation
    [corrected].
  findings: []
- id: PMID:2049874
  title: Ras-related genes in Dictyostelium discoideum.
  findings: []
- id: PMID:20833893
  title: Ras proteins have multiple functions in vegetative cells of Dictyostelium.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: PubMed-verified; defines three distinct non-overlapping RasG
      functions in vegetative cells (cytokinesis, folate chemotaxis, actin/random
      motility).
- id: PMID:23132928
  title: Delineating the core regulatory elements crucial for directed cell migration
    by examining folic-acid-mediated responses.
  findings: []
- id: PMID:23135995
  title: Daydreamer, a Ras effector and GSK-3 substrate, is important for directional
    sensing and cell motility.
  findings: []
- id: PMID:23843627
  title: Two distinct functions for PI3-kinases in macropinocytosis.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: PubMed-verified; RasG binds PI3K1/2 and PI3K4, and single rasG
      mutants have severe macropinocytosis defects.
- id: PMID:24036346
  title: Dictyostelium lipid droplets host novel proteins.
  findings: []
- id: PMID:24338482
  title: Degradation of activated K-Ras orthologue via K-Ras-specific lysine residues
    is required for cytokinesis.
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: PubMed-verified; shows RasG is polyubiquitinated/degraded (a
      substrate), which does not support a ubiquitin-binding molecular function.
- id: PMID:24742374
  title: RasG signaling is important for optimal folate chemotaxis in Dictyostelium.
  findings: []
- id: PMID:24986648
  title: Regulation of a LATS-homolog by Ras GTPases is important for the control
    of cell division.
  findings: []
- id: PMID:27009206
  title: The novel RacE-binding protein GflB sharpens Ras activity at the leading
    edge of migrating cells.
  findings: []
- id: PMID:27172998
  title: The small GTPases Ras and Rap1 bind to and control TORC2 activity.
  findings: []
- id: PMID:27821733
  title: A Diaphanous-related formin links Ras signaling directly to actin assembly
    in macropinocytosis and phagocytosis.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: PubMed-verified; RasG (and RasB) directly regulate the formin ForG
      at endocytic cups, linking Ras to actin assembly in large-scale endocytosis.
- id: PMID:28183814
  title: Comparative Proteomics of Purified Pathogen Vacuoles Correlates Intracellular
    Replication of Legionella pneumophila with the Small GTPase Ras-related protein
    1 (Rap1).
  findings: []
- id: PMID:29109256
  title: GPCR-controlled membrane recruitment of negative regulator C2GAP1 locally
    inhibits Ras signaling for adaptation and long-range chemotaxis.
  findings: []
- id: PMID:30462573
  title: An endogenous chemorepellent directs cell movement by inhibiting pseudopods
    at one side of cells.
  findings: []
- id: PMID:30622175
  title: IQGAP-related protein IqgC suppresses Ras signaling during large-scale endocytosis.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: PubMed-verified; IqgC is a RasG-specific GAP that interacts with
      active RasG during macropinocytosis and phagocytosis.
- id: PMID:30967009
  title: Function of small GTPases in Dictyostelium macropinocytosis.
  findings: []
- id: PMID:34788129
  title: A chemorepellent inhibits local Ras activation to inhibit pseudopod formation
    to bias cell movement away from the chemorepellent.
  findings: []
- id: PMID:38263885
  title: IqgC is a potent regulator of macropinocytosis in the presence of NF1 and
    its loading to macropinosomes is dependent on RasG.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: PubMed-verified; RasG is a major regulator of macropinocytosis and
      recruits IqgC to forming macropinocytic cups.
- id: PMID:38888895
  title: Leep2A and Leep2B function as a RasGAP complex to regulate macropinosome
    formation.
  findings: []
- id: PMID:39458259
  title: 'Francisella novicida-Containing Vacuole within Dictyostelium discoideum:
    Isolation and Proteomic Characterization.'
  findings: []
- id: PMID:39789437
  title: The IQGAP-related RasGAP IqgC regulates cell-substratum adhesion in Dictyostelium
    discoideum.
  findings: []
- id: PMID:40934557
  title: The Ras association domain of DydA as a specific reporter of activated RasG
    in Dictyostelium.
  findings: []
- id: PMID:8754814
  title: Overexpression of an activated rasG gene during growth blocks the initiation
    of Dictyostelium development.
  findings: []
- id: PMID:9245789
  title: Dictyostelium RasG is required for normal motility and cytokinesis, but not
    growth.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: PubMed-verified full text; rasG-null cells have defective motility,
      actin/polarity defects, and fail cytokinesis (become multinucleate in
      suspension).
- id: PMID:9551080
  title: Negative influence of RasG on chemoattractant-induced ERK2 phosphorylation
    in Dictyostelium.
  findings: []
core_functions:
- description: RasG is a plasma-membrane-anchored Ras small GTPase that acts as a
    nucleotide-dependent molecular switch. Upon chemoattractant (folate/cAMP)
    stimulation it is rapidly and transiently loaded with GTP at the cell cortex and
    leading edge, where active RasG transduces the signal to downstream effectors;
    its intrinsic GTPase activity (accelerated by RasGAPs such as IqgC, C2GAP1,
    Leep2 and NF1) resets the switch.
  molecular_function:
    id: GO:0003925
    label: G protein activity
  locations:
  - id: GO:0005886
    label: plasma membrane
  - id: GO:0031252
    label: cell leading edge
  - id: GO:0009898
    label: cytoplasmic side of plasma membrane
  directly_involved_in:
  - id: GO:0007264
    label: small GTPase-mediated signal transduction
  supported_by:
  - reference_id: PMID:15534002
    supporting_text: Ras is rapidly and transiently activated in response to
      chemoattractant stimulation and regulates PI3K activity
  - reference_id: PMID:15143344
    supporting_text: the Ras-binding domain (RBD) of mammalian Raf1 was capable of
      binding to the activated form of RasG
- description: Active GTP-RasG binds and activates class I phosphatidylinositol
    3-kinase (PI3K1/2, PI3K4), generating a localized PIP3 patch at the leading
    edge/cortex that drives F-actin-based pseudopod formation, directional sensing
    and PKB(Akt) activation. This RasG-PI3K axis underlies chemotaxis (to folate and
    cAMP), random motility, cell polarity and macropinocytosis.
  molecular_function:
    id: GO:0035014
    label: phosphatidylinositol 3-kinase regulator activity
  locations:
  - id: GO:0031252
    label: cell leading edge
  - id: GO:0044354
    label: macropinosome
  directly_involved_in:
  - id: GO:0051897
    label: positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal
      transduction
  supported_by:
  - reference_id: PMID:23132928
    supporting_text: Ras and phosphoinositide 3-kinase activity were significantly
      decreased in Ras G and Ras C/G nulls
  - reference_id: PMID:15534002
    supporting_text: chemoattractant-induced Akt/PKB activation was decreased in
      rasG null cells
- description: RasG directly engages effectors that couple its activation to actin
    remodeling and bulk endocytosis, most prominently binding class I PI3-kinases and
    directly regulating the Diaphanous-related formin ForG at endocytic cups. Through
    these effectors RasG is a principal driver of macropinocytosis and phagocytosis
    and of the actin reorganization required for cytokinesis and cell motility.
  molecular_function:
    id: GO:0043548
    label: phosphatidylinositol 3-kinase binding
  locations:
  - id: GO:0044354
    label: macropinosome
  - id: GO:0001891
    label: phagocytic cup
  directly_involved_in:
  - id: GO:0044351
    label: macropinocytosis
  supported_by:
  - reference_id: PMID:23843627
    supporting_text: RasG and RasS interact most strongly with PI3K1/2 and PI3K4
  - reference_id: PMID:27821733
    supporting_text: ForG is directly regulated in large-scale endocytosis by RasB
      and RasG, which are highly related to the human proto-oncogene KRas