rasC

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0003924 GTPase activity	IBA GO_REF:0000033	ACCEPT	Summary: RasC is a Ras-family small GTPase with intrinsic GTPase activity that hydrolyzes bound GTP; this is a core molecular function conserved across the Ras subfamily. Reason: Intrinsic GTPase activity is a defining, well-supported feature of Ras subfamily proteins and is consistent with the UniProt record (EC 3.6.5.2) and the biochemical framing of RasC as a GDP/GTP molecular switch. 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: RasC is a prenylated (geranylgeranylated) protein anchored to the plasma membrane, where activated RasC is enriched at the leading edge of chemotaxing cells. Reason: Plasma-membrane localization is expected for a lipid-anchored Ras GTPase and is consistent with the leading-edge enrichment of active Ras in migrating cells. Supporting Evidence: PMID:20493808 active Ras is enriched at the leading edge of chemotaxing cells
GO:0007264 small GTPase-mediated signal transduction	IBA GO_REF:0000033	ACCEPT	Summary: RasC functions as a small GTPase molecular switch transducing extracellular (chemoattractant) signals to downstream effector pathways. Reason: This is the core biological process for RasC, which relays G-protein-coupled receptor signals to adenylyl cyclase and the TORC2-PKB pathway. Supporting Evidence: PMID:17380187 Ras proteins are small, monomeric GTPases that act as crucial regulators of a number of cellular signalling pathways
GO:0000281 mitotic cytokinesis	IBA GO_REF:0000033	REMOVE	Summary: The cytokinesis inference conflicts with direct functional comparisons of Dictyostelium Ras paralogs: RasD can replace RasG for cytokinesis, whereas RasC cannot. Reason: PTHR24070-paint.tsv places GO:0000281 at PTN001177391 from experimental Dictyostelium descendants DDB_G0292996, DDB_G0292998 and DDB_G0293434. The challenge concerns propagation across the RasC branch, not the number of donors. PMID:20833893 directly compares rasG, rasC/rasG and RasD-rescued strains and finds no RasC contribution to the cytokinesis phenotype, while RasD substitutes for RasG. This target-specific paralog comparison provides positive evidence of functional divergence beyond the relatively normal rasC single knockout. Propagation Review Root cause: PROPAGATION BAD Failure modes: WRONG ORTHOLOG OR PARALOG Sources checked: PANTHER:PTN001177391 · PTN001177391 SUPPORTS SOURCE BUT NOT TARGET The node-level cytokinesis assertion covers the Ras family, but the primary RasG/RasC/RasD comparison (PMID:20833893) distinguishes RasC from the cytokinesis-competent paralogs. Supporting Evidence: PMID:20833893 RasD is capable of totally substituting for RasG for cytokinesis and growth in suspension, whereas RasC is without effect.
GO:0044351 macropinocytosis	IBA GO_REF:0000033	UNDECIDED	Summary: RasC effects on fluid uptake vary by strain and assay, and increased uptake after deletion does not by itself exclude participation in macropinocytosis. Reason: PTHR24070-paint.tsv places GO:0044351 at PTN001177391. The earlier review treated this process annotation as necessarily a positive-regulation claim and used increased liquid-phase endocytosis to refute it. The term itself denotes macropinocytic uptake, and the effects of RasC may be indirect, inhibitory or condition-dependent. Published work reports both increased/normal uptake and a lesser fluid-uptake defect in different contexts. Adjudication must distinguish RasC action in macropinocytic machinery from regulation or compensation before judging the ancestral placement. The completed OpenScientist report recommends removal but incorrectly states that no rasC deletion/fluid-uptake dataset exists. PMID:15878331 directly reports increased liquid-phase endocytosis in rasC-null cells. The report usefully distinguishes pan-Ras reporters and identifies RasG/RasS/RasB effector mechanisms, but their positive roles and RasC failure to rescue RasG-dependent suspension growth do not by themselves establish that RasC lacks an inhibitory or context-dependent macropinocytic role. The process annotation is not restricted to positive regulation. Retain UNDECIDED pending expert reconciliation of uptake phenotypes, cup-specific function and compensation; no duplicate report is needed. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN001177391 · PTN001177391 UNRESOLVED The cached PAINT IBD at this node was checked. RasC effects on fluid uptake vary by strain and assay, and increased uptake after deletion does not by itself exclude participation in macropinocytosis. The prior categorical propagation-error assignment is withdrawn pending assessment of retention versus target-specific divergence. Supporting Evidence: PMID:15878331 These increases were associated with increased liquid phase endocytosis. file:DICDI/rasC/rasC-hypotheses/function-hypothesis-go-0044351/openscientist.md there is no such deletion-uptake dataset in evidence either way
GO:0003925 G protein activity	IEA GO_REF:0000003	ACCEPT	Summary: RasC is a small monomeric GTPase (G protein), consistent with the EC 3.6.5.2 mapping used for this electronic annotation. Reason: RasC is a bona fide Ras-family small GTPase functioning as a nucleotide-dependent molecular switch; the EC-to-GO mapping is appropriate. Supporting Evidence: PMID:15143344 The Ras subfamily consists of small, monomeric GTPases that act as molecular switches in cellular signalling events
GO:0005525 GTP binding	IEA GO_REF:0000002	ACCEPT	Summary: RasC binds guanine nucleotides (GTP/GDP), cycling between active GTP-bound and inactive GDP-bound states. Reason: GTP binding is a defining feature of Ras GTPases and is directly supported by the demonstration that RasC is activated (GTP-loaded) in response to cAMP. Supporting Evidence: PMID:15143344 it was shown that RasC was activated in aggregation-competent cells in response to cAMP
GO:0003924 GTPase activity	IEA GO_REF:0000002	ACCEPT	Summary: InterPro2GO inference of GTPase activity from the small-GTPase domain; correct and consistent with the IBA GTPase annotation. Reason: RasC possesses intrinsic GTPase activity as a Ras-family small GTPase. 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	IEA GO_REF:0000044	ACCEPT	Summary: UniProt subcellular-location mapping to plasma membrane, consistent with the C-terminal prenyl (geranylgeranyl) lipid anchor and leading-edge localization of active RasC. Reason: Membrane localization is expected for a lipid-anchored Ras GTPase; this duplicates the IBA plasma membrane annotation. Supporting Evidence: PMID:20493808 active Ras is enriched at the leading edge of chemotaxing cells
GO:0007165 signal transduction	IEA GO_REF:0000002	ACCEPT	Summary: General signal transduction term consistent with RasC's role as a signaling GTPase; correct but non-specific relative to more informative child terms. Reason: RasC is a signaling molecular switch; the term is accurate though general. Supporting Evidence: PMID:11500376 RasC appears to function as a regulatory molecule for both the cAMP relay and the chemotactic response to cAMP.
GO:0016020 membrane	IEA GO_REF:0000002	KEEP AS NON CORE	Summary: Generic membrane localization term, redundant with the more specific plasma membrane annotation. Reason: The parent term "membrane" is correct but uninformative given the specific plasma membrane localization of prenylated RasC. Supporting Evidence: PMID:20493808 active Ras is enriched at the leading edge of chemotaxing cells
GO:0071321 cellular response to cGMP	IGI PMID:18180289 Rap1 activation in response to cAMP occurs downstream of ras...	KEEP AS NON CORE	Summary: RasC (with RasG) is required for cAMP-induced guanylyl cyclase activation during aggregation; the connection to cGMP responses is indirect and predominantly through RasG. Reason: The genetic evidence links RasC/RasG to guanylyl cyclase activation, but cGMP signaling is predominantly a RasG function and is peripheral to RasC's core role in ACA and TORC2 activation. Supporting Evidence: PMID:18180289 guanylyl cyclase activation is also abolished in the
GO:0019887 protein kinase regulator activity	IDA PMID:15878331 Loss of the Dictyostelium RasC protein alters vegetative cel...	KEEP AS NON CORE	Summary: RasC positively regulates the activity of the PKB/Akt kinases (via TORC2), reflected in reduced Akt/PKB and ERK2 phosphorylation in rasC-null cells. Reason: RasC regulates downstream protein kinases indirectly (through TORC2), so a general "protein kinase regulator activity" molecular function is defensible but less informative than its GTPase/TORC2-activation functions. Supporting Evidence: PMID:15878331 ERK2 phosphorylation and reduced Akt/PKB phosphorylation in response to folate
GO:0043491 phosphatidylinositol 3-kinase/protein kinase B signal transduction	IMP PMID:15878331 Loss of the Dictyostelium RasC protein alters vegetative cel...	ACCEPT	Summary: RasC acts upstream of the PI3K/PKB (Akt) pathway; loss of RasC reduces Akt/PKB phosphorylation in response to chemoattractant. Reason: RasC is a genuine upstream activator of PKB signaling (chiefly via TORC2), a core aspect of its function during chemotaxis and aggregation. Supporting Evidence: PMID:15878331 ERK2 phosphorylation and reduced Akt/PKB phosphorylation in response to folate PMID:11500376 RasC appears to be a central regulatory molecule acting downstream of serpentine receptor stimulation by cAMP that is required for two distinct effector pathways: the activation of Akt/PKB through PI3K and the activation of adenylyl cyclase.
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: RasC (redundantly with RasG) is required for AprA chemorepellent responses; rasC-/rasG- double mutants fail to move away from AprA. Reason: The chemorepulsion role is genuine but redundant with RasG and peripheral to RasC's principal roles in ACA and TORC2 activation. Supporting Evidence: PMID:30462573 signal transduction pathways including Ras
GO:0000165 MAPK cascade	IMP PMID:15878331 Loss of the Dictyostelium RasC protein alters vegetative cel...	KEEP AS NON CORE	Summary: RasC influences ERK2/MAPK phosphorylation in a context-dependent manner (reduced in response to folate), although for cAMP relay ERK2 activation is RasC-independent. Reason: The MAPK role is context-dependent and not RasC's core output; during cAMP relay, cAMP-induced ERK2 phosphorylation is unaffected in rasC-null cells. Supporting Evidence: PMID:15878331 ERK2 phosphorylation and reduced Akt/PKB phosphorylation in response to folate
GO:0031932 TORC2 complex	IDA PMID:31263268 Phosphorylated Rho-GDP directly activates mTORC2 kinase towa...	KEEP AS NON CORE	Summary: Activated RasC associates with TORC2 by binding TOR and by forming a RacE-RasC-mTORC2 supercomplex, but RasC is a regulatory GTPase rather than a stoichiometric core subunit of TORC2. Reason: The experiment establishes a regulated RasC-RacE-mTORC2 signaling assembly. Retain this dynamic regulatory association as non-core relative to the defining TORC2 subunits; the existing TORC2 binding and activation annotations capture the central RasC role. Supporting Evidence: PMID:31263268 assembles the RacE-RasC-mTORC2 supercomplex that phosphorylates AKT
GO:1904515 positive regulation of TORC2 signaling	IDA PMID:31263268 Phosphorylated Rho-GDP directly activates mTORC2 kinase towa...	ACCEPT	Summary: GTP-bound RasC, together with phosphorylated GDP-RacE, directly stimulates mTORC2 kinase activity toward AKT. Reason: Positive regulation of TORC2 is a core RasC function, demonstrated by in vitro reconstitution of RasC-dependent mTORC2-mediated AKT phosphorylation. Supporting Evidence: PMID:31263268 assembles the RacE-RasC-mTORC2 supercomplex that phosphorylates AKT
GO:0051593 response to folic acid	IGI PMID:23132928 Delineating the core regulatory elements crucial for directe...	KEEP AS NON CORE	Summary: RasC contributes to folic-acid-stimulated responses in vegetative cells, notably PKB substrate phosphorylation, via the TORC2 pathway. Reason: RasC participates in folate-triggered signaling but this is one of several redundant vegetative-cell roles, secondary to its core aggregation/ACA and TORC2 functions. Supporting Evidence: PMID:23132928 Ras C activates the TORC2 complex, which in turn triggers PKBA and a second PKB homolog, PKBR1
GO:0007165 signal transduction	IMP PMID:11500376 RasC is required for optimal activation of adenylyl cyclase ...	ACCEPT	Summary: RasC is a signaling GTPase required for cAMP relay and chemotactic responses during aggregation. Reason: Signal transduction is accurate for RasC, supported by the aggregation-defective phenotype of rasC-null cells and their role in cAMP signaling. Supporting Evidence: PMID:11500376 RasC appears to function as a regulatory molecule for both the cAMP relay and the chemotactic response to cAMP.
GO:0007188 adenylate cyclase-modulating G protein-coupled receptor signaling pathway	IMP PMID:15143344 Chemoattractant-induced Ras activation during Dictyostelium ...	ACCEPT	Summary: RasC is activated downstream of the cAMP GPCR and is required for chemoattractant-induced activation of adenylyl cyclase (the cAMP relay). Reason: This is a core function of RasC - transducing cAMP-receptor signals to adenylyl cyclase during aggregation. Supporting Evidence: PMID:15143344 it was shown that RasC was activated in aggregation-competent cells in response to cAMP PMID:17380187 RasG regulates chemotaxis and RasC is responsible for adenylyl cyclase activation
GO:1903665 negative regulation of asexual reproduction	IMP PMID:34154396 An Autocrine Negative Feedback Loop Inhibits Dictyostelium d...	KEEP AS NON CORE	Summary: RasC is required for extracellular-polyphosphate-mediated inhibition of cell proliferation under low-nutrient conditions. Reason: RasC participates in the polyphosphate proliferation-inhibition pathway, but this is a specialized, redundant signaling role distinct from its core aggregation/TORC2 functions. Supporting Evidence: PMID:34154396 the loss of GrlD or RasC blocked the sensitivity of cells to polyphosphate
GO:0051291 protein heterooligomerization	IDA PMID:33238110 Hetero-oligomerization of Rho and Ras GTPases Connects GPCR ...	KEEP AS NON CORE	Summary: Chemoattractant stimulation induces GTP-bound RasC to hetero-oligomerize with phosphorylated GDP-bound RacE, an interaction required for mTORC2-AKT activation. Reason: The RasC-RacE hetero-oligomerization is a genuine, directly demonstrated interaction, but it is a mechanistic step in TORC2 activation rather than a stand-alone core function. Supporting Evidence: PMID:33238110 these two GTPases directly interact in cells
GO:0003925 G protein activity	IDA PMID:17380187 Cyclic AMP signalling in Dictyostelium: G-proteins activate ...	ACCEPT	Summary: RasC is a small GTPase whose GDP-to-GTP exchange is catalyzed specifically by RasGEFA, confirming its function as a nucleotide-switch G protein. Reason: Direct in vitro nucleotide-exchange and activation assays establish RasC as a functional Ras-family G protein. Supporting Evidence: PMID:17380187 RasGEFA catalysed the removal of GDP from RasC but not from other Ras subfamily proteins, confirming that RasGEFA is specific for RasC
GO:0003925 G protein activity	IMP PMID:23132928 Delineating the core regulatory elements crucial for directe...	ACCEPT	Summary: RasC functions as an activatable G protein upstream of the TORC2-PKB pathway in chemotactic responses. Reason: Consistent with the direct IDA evidence that RasC is a Ras-family G protein; this genetic annotation supports the same molecular function. Supporting Evidence: PMID:23132928 Ras C activates the TORC2 complex, which in turn triggers PKBA and a second PKB homolog, PKBR1
GO:0005515 protein binding	IPI PMID:31263268 Phosphorylated Rho-GDP directly activates mTORC2 kinase towa...	MODIFY	Summary: RasC binds the TORC2 signaling machinery; a specific complex-binding term captures this functional interaction. Reason: The cited experiment identifies the TORC2 interaction underlying RasC-dependent kinase activation. Replace generic protein binding with TORC2 complex binding, consistent with the independent direct annotation already present. Proposed replacements: TORC2 complex binding Supporting Evidence: PMID:31263268 assembles the RacE-RasC-mTORC2 supercomplex that phosphorylates AKT
GO:0007265 Ras protein signal transduction	IMP PMID:15878331 Loss of the Dictyostelium RasC protein alters vegetative cel...	ACCEPT	Summary: RasC-mediated signal transduction affects motility, polarity, endocytosis, and chemotactic responses in vegetative and developing cells. Reason: Ras protein signal transduction is the core process RasC executes as a signaling GTPase. Supporting Evidence: PMID:15878331 loss of signal transduction through the RasC protein was found to
GO:0007265 Ras protein signal transduction	IMP PMID:20660630 Ras-mediated activation of the TORC2-PKB pathway is critical...	ACCEPT	Summary: RasC signal transduction controls the TORC2-PKB pathway governing chemotaxis. Reason: Directly supported - RasC is the upstream Ras controlling TORC2-PKB signaling during chemotaxis. Supporting Evidence: PMID:20660630 RasC is required for TORC2-mediated activation of PKB
GO:0106070 regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway	IMP PMID:11500376 RasC is required for optimal activation of adenylyl cyclase ...	ACCEPT	Summary: RasC regulates cAMP-receptor-mediated activation of adenylyl cyclase; rasC-null cells fail to produce cAMP in response to receptor stimulation. Reason: Regulation of the adenylyl-cyclase-activating GPCR pathway is a core RasC function underlying the cAMP relay during aggregation. Supporting Evidence: PMID:11500376 RasC appears to be a central regulatory molecule acting downstream of serpentine receptor stimulation by cAMP that is required for two distinct effector pathways: the activation of Akt/PKB through PI3K and the activation of adenylyl cyclase.
GO:0005515 protein binding	IPI PMID:24986648 Regulation of a LATS-homolog by Ras GTPases is important for...	MODIFY	Summary: RasC binds the LATS-family kinase NdrC, with lower affinity than RasG and RasB. Reason: The yeast two-hybrid and pull-down experiments identify a kinase interaction, supporting protein kinase binding. This molecular interaction alone does not establish a cytokinesis role for RasC. Proposed replacements: protein kinase binding Supporting Evidence: PMID:24986648 NdrC was the only protein that bound RasC in the yeast two-hybrid screen
GO:0005515 protein binding	IPI PMID:26424797 PP2A/B56 and GSK3/Ras suppress PKB activity during Dictyoste...	MODIFY	Summary: GDP-bound RasC associates with the PP2A regulatory subunit B56. Reason: Binding to a defined phosphatase-complex subunit supports protein phosphatase binding, which is more informative than generic protein binding. This preserves the measured interaction and its regulatory context. Proposed replacements: protein phosphatase binding Supporting Evidence: PMID:26424797 GDP forms of RasC and RasD, but not with RasG in vitro
GO:0005515 protein binding	IPI PMID:27172998 The small GTPases Ras and Rap1 bind to and control TORC2 act...	MODIFY	Summary: RasC binds the TORC2 signaling machinery; a specific complex-binding term captures this functional interaction. Reason: The cited experiment identifies the TORC2 interaction underlying RasC-dependent kinase activation. Replace generic protein binding with TORC2 complex binding, consistent with the independent direct annotation already present. Proposed replacements: TORC2 complex binding Supporting Evidence: PMID:27172998 we found that TOR kinase itself specifically co-purifies with RasCGppNHp
GO:0005515 protein binding	IPI PMID:29109256 GPCR-controlled membrane recruitment of negative regulator C...	REMOVE	Summary: The negative regulator C2GAP1 (a RasGAP) binds RasC in vitro, consistent with its role in terminating Ras signaling for adaptation. Reason: The cited interaction is retained as evidence in this review, but the generic protein binding term does not describe the GTPase molecular-switch function. Removal concerns the uninformative annotation, not the validity of the reported interaction; no unsupported replacement function is inferred from binding alone. Supporting Evidence: PMID:29109256 the in vitro binding assay indicates that C2GAP1 binds both GTP- and GDP-bound Ras protein
GO:0005525 GTP binding	IDA PMID:15143344 Chemoattractant-induced Ras activation during Dictyostelium ...	ACCEPT	Summary: RasC binds and is activated by GTP; an RBD-based assay directly detected GTP-loaded (active) RasC upon cAMP stimulation. Reason: Direct experimental demonstration of RasC nucleotide binding/activation supports the GTP-binding molecular function. Supporting Evidence: PMID:15143344 it was shown that RasC was activated in aggregation-competent cells in response to cAMP
GO:0005811 lipid droplet	HDA PMID:24036346 Dictyostelium lipid droplets host novel proteins.	KEEP AS NON CORE	Summary: The curated experimental annotation reports RasC in a lipid droplet preparation; retain this as a secondary localization. Reason: An experimental lipid droplet annotation reports localization and does not require demonstration of a dedicated RasC function in that compartment. The prior review inferred contamination from RasC membrane anchoring without target-specific evidence. The primary plasma-membrane role does not exclude a secondary compartment. Retain the curated observation as non-core and distinguish it from the best-characterized signaling location.
GO:0010856 adenylate cyclase activator activity	IGI PMID:18180289 Rap1 activation in response to cAMP occurs downstream of ras...	ACCEPT	Summary: RasC (with RasG) is required for cAMP-receptor-mediated activation of adenylyl cyclase during aggregation, with RasC being the more important of the two for ACA activation. Reason: Activation of adenylyl cyclase is a core RasC function underlying the cAMP relay; RasC/RasG are the presumptive GTPases required for cyclase activation. Supporting Evidence: PMID:18180289 proteins that are necessary for optimum cAMP signaling PMID:17380187 RasG regulates chemotaxis and RasC is responsible for adenylyl cyclase activation
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- cells, identifying RasC/RasG as required for cyclase activation; however, RasG predominates for the cGMP branch. Reason: RasC contributes to guanylyl cyclase activation but this is largely a RasG-dominated function and secondary to RasC's principal ACA/TORC2 roles. Supporting Evidence: PMID:18180289 guanylyl cyclase activation is also abolished in the
GO:0030250 guanylate cyclase activator activity	IGI PMID:18180289 Rap1 activation in response to cAMP occurs downstream of ras...	KEEP AS NON CORE	Summary: Genetic-interaction evidence that RasC (with RasG) is required for guanylyl cyclase activation; duplicate of the IMP annotation. Reason: Same rationale as the paired IMP annotation - a redundant, RasG-dominated function. Supporting Evidence: PMID:18180289 guanylyl cyclase activation is also abolished in the
GO:0031252 cell leading edge	IC PMID:20493808 A Ras signaling complex controls the RasC-TORC2 pathway and ...	ACCEPT	Summary: Active RasC signaling (RasC-TORC2) is localized to the leading edge of chemotaxing cells, where the Sca1/RasGEF complex promotes local RasC activation. Reason: Leading-edge localization of active RasC signaling is a core spatial feature underlying directed migration. Supporting Evidence: PMID:20493808 active Ras is enriched at the leading edge of chemotaxing cells
GO:0031982 vesicle	IDA PMID:19589376 Nanovesicles released by Dictyostelium cells: a potential ca...	KEEP AS NON CORE	Summary: The curated experimental annotation reports RasC in a vesicle preparation; retain this as a secondary localization. Reason: An experimental vesicle annotation reports localization and does not require demonstration of a dedicated RasC function in that compartment. The prior review inferred contamination from RasC membrane anchoring without target-specific evidence. The primary plasma-membrane role does not exclude a secondary compartment. Retain the curated observation as non-core and distinguish it from the best-characterized signaling location.
GO:0051602 response to electrical stimulus	IMP PMID:26012633 A large-scale screen reveals genes that mediate electrotaxis...	KEEP AS NON CORE	Summary: RasC contributes to electrotaxis through the TORC2-PKB pathway. Reason: The primary abstract explicitly reports decreased electrotaxis in rasC mutants together with several other TORC2-PKB pathway mutants. This is a supported secondary stimulus-response context, not merely an unspecified screen hit. Supporting Evidence: PMID:26012633 electrotaxis was decreased in mutants lacking gefA, rasC, rip3, lst8, or pkbR1
GO:1904841 TORC2 complex binding	IDA PMID:20660630 Ras-mediated activation of the TORC2-PKB pathway is critical...	ACCEPT	Summary: TORC2 binds specifically to the activated (GTP-bound) form of RasC, as shown by co-immunoprecipitation with the TORC2 component Rip3. Reason: Direct binding of activated RasC to TORC2 is a core molecular function central to RasC-mediated PKB activation and chemotaxis. Supporting Evidence: PMID:20660630 This result shows that RasC and TORC2 interact in a regulated fashion
GO:0005515 protein binding	IPI PMID:27009206 The novel RacE-binding protein GflB sharpens Ras activity at...	REMOVE	Summary: The RacE-binding, RhoGAP/RasGEF-domain protein GflB binds RasC (and RasG), linking directional sensing to Ras/Rho activity at the leading edge. Reason: The cited interaction is retained as evidence in this review, but the generic protein binding term does not describe the GTPase molecular-switch function. Removal concerns the uninformative annotation, not the validity of the reported interaction; no unsupported replacement function is inferred from binding alone. Supporting Evidence: PMID:27009206 GflB also binds to Ras GTPases
GO:0110094 polyphosphate-mediated signaling	IMP PMID:28584190 Extracellular polyphosphate signals through Ras and Akt to p...	KEEP AS NON CORE	Summary: RasC (with Akt/PKB) mediates extracellular-polyphosphate signaling that primes cells for development and inhibits the proteasome. Reason: RasC participates in polyphosphate signaling, but this is a specialized branch secondary to its core aggregation and TORC2 roles. Supporting Evidence: PMID:28584190 mediated by Akt proteins and RasC in Dictyostelium
GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction	IMP PMID:20660630 Ras-mediated activation of the TORC2-PKB pathway is critical...	ACCEPT	Summary: RasC positively regulates PKB activation, primarily through TORC2-mediated phosphorylation of PKBR1/PKBA (largely PIP3-independent). Reason: Positive regulation of PKB signaling is a core RasC output; RasC deletion reduces, and activated RasC prolongs, PKB phosphorylation. Supporting Evidence: PMID:20660630 RasC is required for TORC2-mediated activation of PKB
GO:0061122 positive regulation of positive chemotaxis to cAMP	IMP PMID:20660630 Ras-mediated activation of the TORC2-PKB pathway is critical...	KEEP AS NON CORE	Summary: Proper temporal control of RasC-TORC2-PKBR1 signaling is required for efficient directed migration toward cAMP; dysregulated RasC impairs chemotaxis. Reason: RasC contributes to cAMP chemotaxis via TORC2, but chemotactic gradient sensing is dominated by RasG/PI3K; RasC's contribution here is modulatory. Supporting Evidence: PMID:20660630 RasC is required for TORC2-mediated activation of PKB
GO:1904515 positive regulation of TORC2 signaling	IMP PMID:20660630 Ras-mediated activation of the TORC2-PKB pathway is critical...	ACCEPT	Summary: RasC is required for and, when constitutively active, prolongs TORC2-mediated PKB signaling. Reason: Positive regulation of TORC2 is a core RasC function established by genetic and in vitro reconstitution evidence. Supporting Evidence: PMID:20660630 RasC is required for TORC2-mediated activation of PKB
GO:0048870 cell motility	IMP PMID:15878331 Loss of the Dictyostelium RasC protein alters vegetative cel...	KEEP AS NON CORE	Summary: Vegetative rasC-null cells show reduced random motility and are less polarized, indicating a role for RasC in cell motility. Reason: RasC affects motility, but the dominant motility/polarity regulator among the Ras proteins is RasG; RasC's contribution is partial. Supporting Evidence: PMID:15878331 reduced random motility, were less polarized and had altered F-actin
GO:0019954 asexual reproduction	IGI PMID:18180289 Rap1 activation in response to cAMP occurs downstream of ras...	KEEP AS NON CORE	Summary: RasC is required (with RasG) for aggregation, the developmental process that leads to asexual sporulation. Reason: The link to asexual reproduction is via RasC's role in aggregation/cAMP signaling rather than a distinct reproductive function. Supporting Evidence: PMID:18180289 proteins that are necessary for optimum cAMP signaling
GO:0043326 chemotaxis to folate	IGI PMID:20833893 Ras proteins have multiple functions in vegetative cells of ...	KEEP AS NON CORE	Summary: RasC can partially substitute for RasG in folate chemotaxis; rasC-/rasG- cells are completely incapable of folate chemotaxis. Reason: RasC contributes to folate chemotaxis but redundantly with (and secondarily to) RasG. Supporting Evidence: PMID:20833893 to folate, RasC is capable of partially substituting for RasG
GO:0043327 chemotaxis to cAMP	IGI PMID:18180289 Rap1 activation in response to cAMP occurs downstream of ras...	KEEP AS NON CORE	Summary: RasC (with RasG) is required for optimal cAMP signaling that underlies chemotaxis during aggregation. Reason: RasC contributes to cAMP chemotaxis but the chemotactic branch is predominantly RasG-dependent; RasC's core role is ACA activation. Supporting Evidence: PMID:18180289 proteins that are necessary for optimum cAMP signaling
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: RasC (with RasG) acts upstream of PKB activation during cAMP signaling. Reason: Positive regulation of PKB activation is a core RasC output during cAMP signaling, consistent with the reduced PKB phosphorylation of rasC-null cells. Supporting Evidence: PMID:18180289 proteins that are necessary for optimum cAMP signaling
GO:0031152 aggregation involved in sorocarp development	IMP PMID:16885420 Delineation of the roles played by RasG and RasC in cAMP-dep...	ACCEPT	Summary: RasC is required for aggregation, controlling both cAMP relay (ACA activation) and, partly, chemotaxis during early development. Reason: Aggregation is a core developmental process requiring RasC; rasC-null cells fail to aggregate. Supporting Evidence: PMID:16885420 the Ras protein RasC is involved in both processes
GO:0031152 aggregation involved in sorocarp development	IGI PMID:16885420 Delineation of the roles played by RasG and RasC in cAMP-dep...	ACCEPT	Summary: Genetic-interaction evidence (RasC vs RasG) confirming RasC's role in aggregation, predominantly via ACA activation. Reason: Duplicate line of evidence for RasC's core aggregation function. Supporting Evidence: PMID:16885420 signal transduction through RasC is more important in ACA activation
GO:0043327 chemotaxis to cAMP	IMP PMID:16885420 Delineation of the roles played by RasG and RasC in cAMP-dep...	KEEP AS NON CORE	Summary: RasC contributes to cAMP chemotaxis, though signaling through RasG is more important for chemotaxis while RasC is more important for the cAMP relay. Reason: RasC's chemotactic contribution is secondary to RasG; its core role is ACA activation. Supporting Evidence: PMID:16885420 signal transduction through RasC is more important in ACA activation
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: RasC contributes to cAMP-stimulated PKB phosphorylation during aggregation. Reason: Positive regulation of PKB is a core RasC output; this is consistent supporting evidence from the isogenic RasC/RasG null comparison. Supporting Evidence: PMID:16885420 signal transduction through RasC is more important in ACA activation
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 evidence that RasC contributes to PKB activation during aggregation. Reason: Positive regulation of PKB is a core RasC output; consistent supporting evidence. Supporting Evidence: PMID:16885420 signal transduction through RasC is more important in ACA activation
GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction	IMP PMID:11500376 RasC is required for optimal activation of adenylyl cyclase ...	ACCEPT	Summary: cAMP-induced Akt/PKB phosphorylation through a PI3K-dependent pathway is dramatically reduced in rasC-null cells. Reason: RasC positively regulating PKB activation is a core function, directly demonstrated by reduced Akt/PKB phosphorylation in rasC-null cells. Supporting Evidence: PMID:11500376 RasC appears to be a central regulatory molecule acting downstream of serpentine receptor stimulation by cAMP that is required for two distinct effector pathways: the activation of Akt/PKB through PI3K and the activation of adenylyl cyclase.
GO:0031152 aggregation involved in sorocarp development	IMP PMID:16023096 The effect of the disruption of a gene encoding a PI4 kinase...	ACCEPT	Summary: Disruption of rasC produces a strain that fails to aggregate, with defects in both cAMP signal relay and chemotaxis. Reason: Core developmental phenotype - RasC is required for aggregation. Supporting Evidence: PMID:16023096 fails to aggregate with defects in both cAMP
GO:0043327 chemotaxis to cAMP	IMP PMID:16023096 The effect of the disruption of a gene encoding a PI4 kinase...	KEEP AS NON CORE	Summary: rasC-null cells are defective in cAMP chemotaxis (as part of the aggregation-negative phenotype). Reason: RasC contributes to cAMP chemotaxis but redundantly with/secondarily to RasG; its core role is ACA activation. Supporting Evidence: PMID:16023096 fails to aggregate with defects in both cAMP
GO:0001558 regulation of cell growth	IMP PMID:15878331 Loss of the Dictyostelium RasC protein alters vegetative cel...	KEEP AS NON CORE	Summary: rasC-null cells contain more protein and are larger than wild type, indicating a role for RasC in regulating cell size/growth. Reason: RasC influences vegetative cell size, but this is one of several secondary vegetative-cell phenotypes rather than a core function. Supporting Evidence: PMID:15878331 Cells lacking RasC also contained more protein and were larger in
GO:0051491 positive regulation of filopodium assembly	IMP PMID:15878331 Loss of the Dictyostelium RasC protein alters vegetative cel...	UNDECIDED	Summary: The available RasC study reports altered F-actin distribution and polarity, but the specific filopodium-assembly assay is not accessible. Reason: The cached record is abstract-only and does not establish the direction or specificity of the filopodium-assembly phenotype. Do not replace the curator's full-text judgment with an inference from a broader actin phenotype. Leave this specific experimental annotation unresolved pending the relevant full text. Supporting Evidence: PMID:15878331 reduced random motility, were less polarized and had altered F-actin
GO:0007163 establishment or maintenance of cell polarity	IMP PMID:15878331 Loss of the Dictyostelium RasC protein alters vegetative cel...	KEEP AS NON CORE	Summary: rasC-null cells are less polarized, indicating a role for RasC in cell polarity. Reason: RasC contributes to polarity/actin organization but is not the dominant polarity regulator among Dictyostelium Ras proteins. Supporting Evidence: PMID:15878331 reduced random motility, were less polarized and had altered F-actin
GO:0030036 actin cytoskeleton organization	IMP PMID:15878331 Loss of the Dictyostelium RasC protein alters vegetative cel...	KEEP AS NON CORE	Summary: Loss of RasC alters F-actin distribution, linking RasC signaling to actin cytoskeleton organization. Reason: RasC influences the actin cytoskeleton (via TORC2-PKB and downstream effectors), a secondary consequence of its signaling rather than a direct core function. Supporting Evidence: PMID:15878331 reduced random motility, were less polarized and had altered F-actin
GO:0043326 chemotaxis to folate	IMP PMID:15878331 Loss of the Dictyostelium RasC protein alters vegetative cel...	KEEP AS NON CORE	Summary: rasC-null cells chemotax poorly to folate and show reduced folate-induced F-actin and PKB responses. Reason: RasC contributes to folate chemotaxis but redundantly with RasG; this is a vegetative-cell role secondary to RasC's core aggregation/ACA function. Supporting Evidence: PMID:15878331 chemotaxed poorly to folate
GO:0120320 lateral pseudopodium retraction	IMP PMID:15878331 Loss of the Dictyostelium RasC protein alters vegetative cel...	UNDECIDED	Summary: This specific term (lateral pseudopodium retraction) is not addressed in the accessible (abstract-only) record for this reference, which reports reduced polarity and altered F-actin but not pseudopod retraction dynamics per se. Reason: The cached publication is abstract-only and does not provide verifiable support for a specific lateral-pseudopodium-retraction function; the curator likely relied on full-text data not accessible here.
GO:0031152 aggregation involved in sorocarp development	IMP PMID:11500376 RasC is required for optimal activation of adenylyl cyclase ...	ACCEPT	Summary: Disruption of rasC generates cells incapable of aggregation, a defect restricted to the aggregation stage and rescuable by exogenous cAMP pulses. Reason: RasC's requirement for aggregation is a core developmental function directly demonstrated by the rasC-null phenotype. Supporting Evidence: PMID:11500376 generated cells incapable of aggregation

Gene Description

Existing Annotations Review

Core Functions

Activated RasC drives the chemoattractant-induced activation of adenylyl cyclase (ACA) and the cAMP relay during aggregation, functioning as the principal Ras protein for the cAMP signal-relay branch downstream of the cAMP GPCR and RasGEFA (Aimless).

GTP-bound RasC binds the TOR catalytic domain and, together with phosphorylated GDP-bound RacE, directly activates TORC2, setting the temporal and spatial dynamics of PKBR1/PKBA (Akt) phosphorylation that control the actin cytoskeleton and directed cell migration.

References

Deep Research

OpenScientist

📚 Additional Documentation

Notes

📄 View Raw YAML