ABI3

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0048858 cell projection morphogenesis	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation based on phylogenetic inference from ABI family orthologs across species. ABI3 is a WRC component and the WRC is essential for actin-dependent cell projection formation. ABI3-containing WAVE2 complexes influence protrusion formation, though ABI3 specifically impairs lamellipodial protrusions while potentially favoring ventral protrusions (PMID:26428302). The term 'cell projection morphogenesis' is appropriately general for this family-level annotation. Reason: As a WRC component, ABI3 modulates actin-dependent cell projections. The IBA annotation at this level of specificity is appropriate given the phylogenetic conservation of this function across ABI family members. Supporting Evidence: PMID:26428302 the formation of peripheral lamellipodial structures was disturbed, suggesting that the NESH/Abi-3-based WAVE2 complex was unable to help produce lamellipodial protrusions
GO:0001764 neuron migration	IBA GO_REF:0000033	KEEP AS NON CORE	Summary: IBA annotation inferred from orthologs. ABI family members participate in neuron migration via actin regulation through the WRC. ABI3 is expressed in the brain, particularly in microglia (not neurons primarily), but WRC function in neuron migration is well-established for ABI1/ABI2 orthologs. Reason: Neuron migration is a conserved function of ABI family members through the WRC. However, ABI3 is primarily enriched in microglia rather than neurons in the brain. The IBA inference from orthologs is phylogenetically reasonable but this is not a core function of ABI3 specifically.
GO:0030027 lamellipodium	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation for lamellipodium localization based on phylogenetic inference. ABI3 localizes to lamellipodia as shown by IDA evidence in PMID:17101133. This is consistent with its role as a WRC component, since the WRC drives Arp2/3-dependent actin polymerization at the leading edge. Reason: Supported by direct experimental evidence (IDA from PMID:17101133) and consistent with ABI3 function as a WRC component. Lamellipodium localization is a core aspect of ABI3 biology. Supporting Evidence: PMID:17101133 Immunoprecipitation revealed that NESH (Abi-3) is present in the Abi/WAVE complex
GO:0031209 SCAR complex	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation for SCAR/WAVE complex membership. This is very well supported by multiple IDA studies (PMID:17101133, PMID:26428302) and IP-MS data (Moraes et al. 2017). ABI3 is a bona fide component of the WAVE regulatory complex, occupying the Abi subunit position. Reason: Core function of ABI3. Membership in the SCAR/WAVE complex is the defining biochemical role of ABI3. Strongly supported by multiple independent experimental studies. Supporting Evidence: PMID:17101133 Immunoprecipitation revealed that NESH (Abi-3) is present in the Abi/WAVE complex. Our results suggest that NESH (Abi-3), like Abi-1 and Abi-2, is a component of the Abi/WAVE complex PMID:26428302 NESH/Abi-3 was ectopically expressed in NIH3T3 cells, in which Abi-1, but not NESH/Abi-3, is expressed. The expression of NESH/Abi-3 caused degradation of endogenous Abi-1, which led to the formation of a NESH/Abi-3-based WAVE2 complex
GO:0035591 signaling adaptor activity	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation for signaling adaptor activity. ABI3 functions as an adaptor protein within the WRC, linking upstream signals to actin cytoskeleton regulation. It contains an SH3 domain and proline-rich regions typical of adaptor proteins. The SH3 domain interacts with PAK and IRSp53 (PMID:11956071, PMID:18480067). Reason: ABI3 is a well-characterized adaptor protein. Its SH3 domain mediates protein-protein interactions and it serves as a bridge within the WRC to couple signaling to actin regulation. This accurately captures the molecular function of ABI3. Supporting Evidence: PMID:11956071 The SH3 domain of NESH seems to interact with p21-activated kinase (PAK), which is involved in regulation of cell motility
GO:0098858 actin-based cell projection	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation for actin-based cell projection localization. ABI3 localizes to actin-based structures as a WRC component. Experimental evidence shows it at lamellipodia and potentially invadopodia (PMID:26428302). Reason: Consistent with ABI3 function as a WRC component that regulates actin-based protrusions. Well-supported by the IDA evidence for lamellipodium localization and the broader role in actin-based structures.
GO:0030334 regulation of cell migration	IBA GO_REF:0000033	ACCEPT	Summary: IBA annotation for regulation of cell migration. Strongly supported by experimental evidence showing that forced expression of NESH/ABI3 suppresses cell motility and metastatic dissemination (PMID:11956071). ABI3 modulates migration through its effects on WRC-dependent actin dynamics. Reason: Core function of ABI3. Regulation of cell migration is one of the best-characterized biological roles of ABI3, supported by multiple independent studies. Supporting Evidence: PMID:11956071 every clone of NESH transfectants caused a marked reduction in motility, although the clones exhibited no significant differences in intrinsic cell growth compared with the control cells in vitro
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: IEA annotation from UniProt subcellular location mapping. Cytoplasmic localization is supported by IDA evidence (GO_REF:0000054) and NAS from PMID:11956071. UniProt states ABI3 localizes to the cytoplasm and colocalizes with PAK2 at the leading edge of cells. Reason: Consistent with experimental evidence for cytoplasmic localization. Broad IEA mapping is acceptable given strong experimental support.
GO:0005515 protein binding	IPI PMID:16189514 Towards a proteome-scale map of the human protein-protein in...	MARK AS OVER ANNOTATED	Summary: Protein binding annotation from high-throughput interactome study. While ABI3 does bind multiple proteins, 'protein binding' is uninformative. The more specific 'signaling adaptor activity' (GO:0035591) already captures the molecular function. Reason: 'Protein binding' is too vague to be informative. ABI3 does bind proteins but the specific adaptor function is better captured by GO:0035591 (signaling adaptor activity). High-throughput interactome data does not provide mechanistic insight.
GO:0005515 protein binding	IPI PMID:17101133 NESH (Abi-3) is present in the Abi/WAVE complex but does not...	MARK AS OVER ANNOTATED	Summary: Protein binding from PMID:17101133 which demonstrated ABI3 interacts with WAVE2 complex components. This is more informative than generic protein binding as it reflects the specific WRC interaction, but the term itself is uninformative. Reason: While the underlying interaction data from PMID:17101133 is high quality and shows specific binding to WAVE complex components, 'protein binding' is not an informative GO term. The SCAR complex membership and signaling adaptor activity annotations better capture this function. Supporting Evidence: PMID:17101133 Immunoprecipitation revealed that NESH (Abi-3) is present in the Abi/WAVE complex
GO:0005515 protein binding	IPI PMID:19060904 An empirical framework for binary interactome mapping.	MARK AS OVER ANNOTATED	Summary: Protein binding from high-throughput binary interactome mapping study. Reason: Generic 'protein binding' from high-throughput study is uninformative. More specific molecular function terms already exist for ABI3.
GO:0005515 protein binding	IPI PMID:21516116 Next-generation sequencing to generate interactome datasets.	MARK AS OVER ANNOTATED	Summary: Protein binding from next-generation sequencing interactome dataset. Reason: Generic 'protein binding' from high-throughput study is uninformative.
GO:0005515 protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	MARK AS OVER ANNOTATED	Summary: Protein binding from proteome-scale interactome mapping. Reason: Generic 'protein binding' from high-throughput study is uninformative.
GO:0005515 protein binding	IPI PMID:27107014 An inter-species protein-protein interaction network across ...	MARK AS OVER ANNOTATED	Summary: Protein binding from inter-species protein-protein interaction network study. Reason: Generic 'protein binding' from high-throughput study is uninformative.
GO:0005515 protein binding	IPI PMID:29892012 An interactome perturbation framework prioritizes damaging m...	MARK AS OVER ANNOTATED	Summary: Protein binding from interactome perturbation framework study. Reason: Generic 'protein binding' from high-throughput study is uninformative.
GO:0005515 protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	MARK AS OVER ANNOTATED	Summary: Protein binding from reference binary protein interactome map. Reason: Generic 'protein binding' from high-throughput study is uninformative.
GO:0005515 protein binding	IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func...	MARK AS OVER ANNOTATED	Summary: Protein binding from multimodal cell maps study. Reason: Generic 'protein binding' from high-throughput study is uninformative.
GO:0042802 identical protein binding	IPI PMID:25416956 A proteome-scale map of the human interactome network.	ACCEPT	Summary: Self-interaction of ABI3 detected in high-throughput interactome study. UniProt interaction data confirms ABI3 self-interaction (NbExp=4). Reason: ABI3 homodimerization is supported by multiple independent high-throughput studies and is recorded in IntAct. This is more informative than generic 'protein binding' and may reflect a functional oligomerization relevant to WRC assembly or regulation.
GO:0042802 identical protein binding	IPI PMID:32296183 A reference map of the human binary protein interactome.	ACCEPT	Summary: Additional evidence for ABI3 self-interaction from reference interactome map. Reason: Independent confirmation of ABI3 homodimerization. Duplicates with different references are acceptable.
GO:0002357 defense response to tumor cell	IEA GO_REF:0000120	KEEP AS NON CORE	Summary: This tumor-response annotation reflects ABI3 re-expression tumor-suppressor phenotypes and automated transfer of that same biology, but it is secondary to ABI3 WRC/adaptor control of actin-dependent protrusion and migration. Reason: Keep as non-core. The tumor-response phenotype is supported in cancer-cell models, but the term is a downstream disease-context consequence rather than the defining ABI3 WAVE regulatory complex adaptor function.
GO:0010593 negative regulation of lamellipodium assembly	IEA GO_REF:0000107	ACCEPT	Summary: IEA annotation transferred from mouse ortholog. Supported by experimental evidence in PMID:26428302 showing that ABI3/NESH expression in NIH3T3 cells reduced WAVE2 translocation to the plasma membrane and disturbed lamellipodial formation. Reason: This is a well-supported function of ABI3. The ABI3-based WAVE2 complex is functionally distinct and impairs lamellipodial protrusion formation compared to ABI1-based complexes. Supporting Evidence: PMID:26428302 the translocation of WAVE2 to the plasma membrane was significantly reduced and the formation of peripheral lamellipodial structures was disturbed
GO:0030027 lamellipodium	IEA GO_REF:0000120	ACCEPT	Summary: IEA annotation for lamellipodium localization. Consistent with IDA evidence from PMID:17101133 and IBA annotation. Reason: Redundant with IBA and IDA annotations but not incorrect. Lamellipodium localization is well established for ABI3.
GO:0031209 SCAR complex	IEA GO_REF:0000120	ACCEPT	Summary: IEA annotation for SCAR complex membership. Consistent with IDA annotations from PMID:17101133 and PMID:26428302. Reason: Core function. Redundant with IDA annotations but acceptable.
GO:0098794 postsynapse	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: IEA annotation transferred from rat ortholog via Ensembl Compara. ISS annotations from ARUK-UCL also support postsynaptic localization (dendritic spine, postsynaptic density). The WRC functions in dendritic spine morphogenesis, supporting synaptic localization. However, ABI3 is primarily enriched in microglia rather than neurons. Reason: While WRC-mediated actin regulation at the postsynapse is conserved for ABI family members, ABI3 is primarily expressed in microglia in the brain, not neurons. The synaptic annotations may be more relevant to ABI1/ABI2 and transferred to ABI3 by orthology. Keep as non-core pending direct evidence in neurons.
GO:0098885 modification of postsynaptic actin cytoskeleton	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: IEA annotation from rat ortholog. WRC-dependent actin modification at postsynapses is a known function of ABI family members. However, ABI3 is primarily microglial rather than neuronal in the brain. Reason: Plausible by orthology and WRC function but ABI3 is not the primary ABI family member in neurons. This function may be more attributable to ABI1/ABI2.
GO:0098978 glutamatergic synapse	IEA GO_REF:0000107	KEEP AS NON CORE	Summary: IEA annotation transferred from rat ortholog. Glutamatergic synapse localization may be more relevant to ABI1/ABI2 given ABI3 enrichment in microglia. Reason: Transferred from rat ortholog. ABI3 is microglia-enriched in brain tissue and not primarily neuronal. This annotation may reflect function of other ABI paralogs rather than ABI3 specifically.
GO:1903077 negative regulation of protein localization to plasma membrane	IEA GO_REF:0000107	ACCEPT	Summary: IEA annotation from mouse ortholog. Supported by experimental evidence showing that ABI3 expression reduces WAVE2 translocation to the plasma membrane (PMID:26428302). Reason: Well-supported by experimental data. ABI3-containing WAVE2 complexes show reduced translocation to the plasma membrane compared to ABI1-containing complexes, consistent with this annotation. Supporting Evidence: PMID:26428302 the translocation of WAVE2 to the plasma membrane was significantly reduced
GO:0030036 actin cytoskeleton organization	ISS GO_REF:0000024	ACCEPT	Summary: ISS annotation transferred by curator judgment. ABI3 participates in actin cytoskeleton organization as a WRC component. The WRC activates Arp2/3-mediated actin nucleation and polymerization. Reason: Core function of ABI3. As a WRC subunit, ABI3 directly participates in actin cytoskeleton organization. Well-supported by multiple studies showing effects on lamellipodia, cell protrusions, and actin-based structures.
GO:0002357 defense response to tumor cell	IMP PMID:21223585 ABI3 ectopic expression reduces in vitro and in vivo cell gr...	KEEP AS NON CORE	Summary: IMP annotation from PMID:21223585 showing that ABI3 ectopic expression reduces tumor growth in vitro and in vivo in thyroid and colon carcinoma cell lines. ABI3 expression is frequently lost in carcinomas, and re-expression reduces transforming activity, anchorage-independent growth, and in vivo tumor formation. Reason: The experimental evidence is solid showing tumor-suppressive effects of ABI3 re-expression. However, 'defense response to tumor cell' is not the most precise term for what was shown. The study demonstrates tumor suppressor activity through re-expression in cancer cells where ABI3 was silenced. This is more accurately described as negative regulation of cell proliferation or tumor suppression. Nevertheless, this is a secondary consequence of ABI3's primary role in actin regulation and cell migration, not a core evolved function. Supporting Evidence: PMID:21223585 Ectopic expression of ABI3 was sufficient to lead to a lower transforming activity, reduced tumor in vitro growth properties, suppressed in vitro anchorage-independent growth and in vivo tumor formation while, cellular senescence increased
GO:2000774 positive regulation of cellular senescence	IMP PMID:21223585 ABI3 ectopic expression reduces in vitro and in vivo cell gr...	KEEP AS NON CORE	Summary: IMP annotation from PMID:21223585. ABI3 ectopic expression induced senescence in thyroid and colon carcinoma cells, accompanied by p21WAF1 upregulation and reduced ERK phosphorylation. Reason: The experimental evidence for senescence induction is clear from PMID:21223585. However, this is likely a secondary consequence of ABI3 re-expression in cancer cells rather than a core evolved function. This effect is observed in the context of ectopic expression in cells where ABI3 was silenced, and the senescence phenotype may reflect disruption of oncogenic signaling rather than a primary ABI3 function. Supporting Evidence: PMID:21223585 cellular senescence increased. These responses were accompanied by the up-regulation of the cell cycle inhibitor p21 WAF1 and reduced ERK phosphorylation and E2F1 expression
GO:0031209 SCAR complex	IDA PMID:17101133 NESH (Abi-3) is present in the Abi/WAVE complex but does not...	ACCEPT	Summary: IDA annotation from PMID:17101133 demonstrating ABI3 is present in the Abi/WAVE complex by immunoprecipitation. This is a key finding establishing ABI3 as a bona fide WRC component. Reason: Core function. Direct experimental evidence from immunoprecipitation showing ABI3 is a component of the WAVE complex. Supporting Evidence: PMID:17101133 Immunoprecipitation revealed that NESH (Abi-3) is present in the Abi/WAVE complex. Our results suggest that NESH (Abi-3), like Abi-1 and Abi-2, is a component of the Abi/WAVE complex
GO:0043197 dendritic spine	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: ISS annotation transferred from a rat ortholog (F1M0R2) by ARUK-UCL curators. WRC components are known to localize to dendritic spines where they regulate spine morphogenesis. However, ABI3 is primarily microglial in the brain. Reason: While WRC function at dendritic spines is conserved for ABI family members, ABI3 is microglia-enriched in the brain. This annotation may primarily reflect the function of ABI1/ABI2 in neurons, transferred by sequence similarity.
GO:0043198 dendritic shaft	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: ISS annotation transferred from rat ortholog. Similar considerations as for dendritic spine localization. Reason: ABI3 is microglia-enriched rather than neuronal. This annotation may reflect function of other ABI paralogs. Keeping as non-core.
GO:0014069 postsynaptic density	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: ISS annotation transferred from rat ortholog. Postsynaptic density localization is well-established for WRC components, but ABI3 is primarily microglial. Reason: Same reasoning as for dendritic spine. WRC function at the PSD is conserved for ABI family but ABI3 enrichment in microglia suggests this is not its primary localization context.
GO:0051015 actin filament binding	ISS GO_REF:0000024	UNDECIDED	Summary: ISS annotation transferred from rat ortholog. ABI3 contains domains that could mediate interactions with actin-based structures, but direct actin filament binding by ABI3 itself has not been demonstrated. ABI3 functions as an adaptor within the WRC rather than directly binding actin filaments. Reason: There is no direct evidence for ABI3 binding actin filaments. ABI3 interacts with actin-regulatory complexes (WRC) but its function is as an adaptor, not an actin-binding protein per se. The ISS transfer may be from a different ABI paralog with distinct biochemical properties. More evidence needed to confirm direct actin filament binding by ABI3.
GO:0061001 regulation of dendritic spine morphogenesis	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: ISS annotation from rat ortholog. WRC regulates dendritic spine morphogenesis but ABI3 is microglia-enriched, not primarily neuronal. Reason: WRC function in spine morphogenesis is well-established but likely mediated by ABI1/ABI2 in neurons. ABI3 is primarily expressed in microglia.
GO:0099151 regulation of postsynaptic density assembly	ISS GO_REF:0000024	KEEP AS NON CORE	Summary: ISS annotation from rat ortholog. Similar considerations as other synaptic annotations. Reason: ABI3 is microglia-enriched and not the primary ABI paralog at neuronal synapses. Keep as non-core.
GO:1900028 negative regulation of ruffle assembly	NAS PMID:18480067 Insulin receptor substrate protein 53 (IRSp53) as a binding ...	ACCEPT	Summary: NAS annotation from PMID:18480067 which identified IRSp53 as a binding partner of NESH/ABI3. The paper is a brief letter identifying the interaction. Previous work showed ABI3 over-expression blocked PDGF-stimulated membrane ruffling. Reason: Negative regulation of ruffle assembly is consistent with ABI3's role in modulating actin-based structures. ABI3 overexpression blocks PDGF-stimulated membrane ruffling, and ABI3-containing WAVE2 complexes impair protrusion formation (PMID:26428302). This is a direct consequence of ABI3's core function in modulating WRC activity. Supporting Evidence: PMID:26428302 the translocation of WAVE2 to the plasma membrane was significantly reduced and the formation of peripheral lamellipodial structures was disturbed
GO:0010593 negative regulation of lamellipodium assembly	ISS GO_REF:0000024	ACCEPT	Summary: ISS annotation from mouse ortholog. Strongly supported by experimental evidence in PMID:26428302 showing ABI3-containing WAVE2 complexes impair lamellipodium formation. Reason: This is a core function distinguishing ABI3 from ABI1/ABI2. ABI3-based WAVE2 complexes are functionally distinct and impair lamellipodial protrusions. Supporting Evidence: PMID:26428302 the NESH/Abi-3-based WAVE2 complex was unable to help produce lamellipodial protrusions
GO:0031209 SCAR complex	IDA PMID:26428302 The NESH/Abi-3-based WAVE2 complex is functionally distinct ...	ACCEPT	Summary: IDA annotation from PMID:26428302 providing detailed characterization of the ABI3-based WAVE2 complex. Demonstrated that ABI3 expression leads to degradation of endogenous ABI1 and formation of an ABI3-based WAVE2 complex. Reason: Core function. Independent confirmation of SCAR/WAVE complex membership with detailed functional characterization of the distinct ABI3-containing complex. Supporting Evidence: PMID:26428302 The expression of NESH/Abi-3 caused degradation of endogenous Abi-1, which led to the formation of a NESH/Abi-3-based WAVE2 complex
GO:1903077 negative regulation of protein localization to plasma membrane	ISS GO_REF:0000024	ACCEPT	Summary: ISS annotation from mouse ortholog. ABI3 expression reduces WAVE2 translocation to the plasma membrane, as shown in PMID:26428302. Reason: Well-supported by experimental data. ABI3-containing WAVE2 complexes show reduced membrane translocation compared to ABI1-containing complexes. Supporting Evidence: PMID:26428302 the translocation of WAVE2 to the plasma membrane was significantly reduced
GO:0016020 membrane	HDA PMID:19946888 Defining the membrane proteome of NK cells.	ACCEPT	Summary: HDA annotation from a study defining the membrane proteome of NK cells. ABI3 was detected in the membrane fraction by proteomics. Reason: ABI3 as a WRC component can associate with membranes, particularly at the leading edge where it colocalizes with PAK2. Detection in membrane proteome of NK cells is consistent with this.
GO:0005737 cytoplasm	IDA GO_REF:0000054	ACCEPT	Summary: IDA annotation from LIFEdb based on intracellular localization of expressed fusion proteins in living cells. Consistent with UniProt subcellular location annotation. Reason: Cytoplasmic localization is well-established for ABI3. Supported by multiple independent evidence sources.
GO:0018108 peptidyl-tyrosine phosphorylation	IDA NOT PMID:17101133 NESH (Abi-3) is present in the Abi/WAVE complex but does not...	ACCEPT	Summary: CORRECT negative annotation. PMID:17101133 explicitly tested and showed that "NESH (Abi-3) had no such effect" on promoting c-Abl-mediated phosphorylation, unlike Abi-1 and Abi-2 which do promote this activity. This negative annotation correctly captures that ABI3/NESH does NOT participate in peptidyl-tyrosine phosphorylation processes. Reason: Important negative annotation that distinguishes ABI3 from its paralogs ABI1 and ABI2. PMID:17101133 directly tested and demonstrated this difference. Supporting Evidence: PMID:17101133 Although Abi-2, like Abi-1, promoted the c-Abl-mediated phosphorylation of Mena and WAVE2, NESH (Abi-3) had no such effect. This difference was likely due to their binding abilities as to c-Abl
GO:0030027 lamellipodium	IDA PMID:17101133 NESH (Abi-3) is present in the Abi/WAVE complex but does not...	ACCEPT	Summary: IDA annotation from PMID:17101133. ABI3 was shown to be present in the Abi/WAVE complex which localizes to lamellipodia where it regulates Rac-dependent actin polymerization. Reason: Direct experimental evidence supports lamellipodium localization of ABI3 as part of the WAVE complex. Supporting Evidence: PMID:17101133 Immunoprecipitation revealed that NESH (Abi-3) is present in the Abi/WAVE complex
GO:0030334 regulation of cell migration	IDA PMID:11956071 Forced expression of NESH suppresses motility and metastatic...	ACCEPT	Summary: IDA annotation from PMID:11956071 showing forced NESH/ABI3 expression suppresses cell motility. NESH transfectants showed marked reduction in motility and reduced tumor metastatic potential in vivo. Reason: Core function. One of the earliest and best-characterized biological roles of ABI3. Direct experimental demonstration of cell migration regulation. Supporting Evidence: PMID:11956071 every clone of NESH transfectants caused a marked reduction in motility, although the clones exhibited no significant differences in intrinsic cell growth compared with the control cells in vitro. The NESH transfectants also exhibited significant reduction in tumor metastatic potential in vivo
GO:0005737 cytoplasm	NAS PMID:11956071 Forced expression of NESH suppresses motility and metastatic...	ACCEPT	Summary: NAS annotation for cytoplasmic localization from PMID:11956071. The paper describes NESH as an intracellular SH3 adapter protein. Reason: Consistent with other evidence for cytoplasmic localization. The paper describes cytoplasmic distribution and colocalization with PAK2 at the leading edge of cells. Supporting Evidence: PMID:11956071 The SH3 domain of NESH seems to interact with p21-activated kinase (PAK), which is involved in regulation of cell motility

Gene Description

Existing Annotations Review

Core Functions

Component of the WAVE regulatory complex (WRC/SCAR complex), occupying the Abi subunit position. ABI3 forms a heteropentameric complex with WAVE2, CYFIP1, NAP1, and BRK1 that couples upstream signals (Rac, Arf GTPases) to Arp2/3-mediated actin nucleation and polymerization.

Negative regulation of lamellipodium assembly and membrane ruffling. ABI3-based WAVE2 complexes specifically impair the formation of peripheral lamellipodial structures, distinguishing ABI3 from ABI1 and ABI2 in terms of protrusion type regulation.

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