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).
| 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 |
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