Affinage

ARAP3

Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 3 · UniProt Q8WWN8

Length
1544 aa
Mass
169.8 kDa
Annotated
2026-06-09
27 papers in source corpus 21 papers cited in narrative 21 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

ARAP3 is a phosphoinositide-regulated dual GTPase-activating protein that converts localized PI3K signaling into coordinated control of Arf6 and RhoA, thereby shaping the actin cytoskeleton, cell adhesion, and vascular morphogenesis (PMID:11804589, PMID:16472652). It is a PtdIns(3,4,5)P3/PtdIns(3,4)P2-stimulated Arf6 GAP and a RhoA-preferring Rho GAP whose Rho GAP activity is switched on by direct binding of GTP-loaded Rap to its Ras-binding domain, with PtdIns(3,4,5)P3-dependent membrane recruitment required to license this Rap-driven activation in cells (PMID:11804589, PMID:15296756, PMID:16472652); the structural basis for its RhoA preference over Rac1 and Cdc42 was resolved in a RhoA-RhoGAP domain co-crystal (PMID:27311713). Membrane recruitment depends on an unusual lipid-binding mode in which tandem N-terminal PH domains, an N-terminal linker, and the SAM domain cooperate, with the first PH domain alone sufficient for specific PtdIns(3,4,5)P3 recognition (PMID:19786092, PMID:36674645). ARAP3 is negatively regulated by Src-family kinase phosphorylation of C-terminal tyrosines (Y1399/Y1404), which creates a docking site bound by the Vav2 SH2 domain (PMID:15546919, PMID:22750419), while its SAM domain mediates heterodimeric interactions with the PtdIns(3,4,5)P3 phosphatase SHIP2 and with Odin (PMID:17314030, PMID:19765305, PMID:23239578). Through these activities ARAP3 enables lamellipodia formation, neurite outgrowth downstream of Rap1, and restrains cell spreading, adhesion, and invasion (PMID:15546919, PMID:16418224, PMID:20578246, PMID:21076469). In vivo it acts as the endothelial PI3Kα effector required for sprouting angiogenesis and lymphangiogenesis, guards neutrophils in a quiescent state by limiting β2 integrin inside-out signaling, and protects against microvascular permeability and NET formation (PMID:20978237, PMID:21490342, PMID:23180820, PMID:38734878).

Mechanistic history

Synthesis pass · year-by-year structured walk · 19 steps
  1. 2002 High

    Established ARAP3 as a phosphoinositide-responsive enzyme by showing it is a PtdIns(3,4,5)P3-stimulated Arf6 GAP whose Arf and Rho GAP domains together drive PI3K-dependent cytoskeletal and cell-shape changes, linking lipid signaling to GTPase control.

    Evidence Phosphoinositide affinity capture and mass spectrometry from leukocyte extracts with in vitro and in vivo GAP assays

    PMID:11804589

    Open questions at the time
    • Did not define the structural basis for lipid binding
    • Rho GAP substrate specificity not yet resolved
  2. 2004 High

    Defined the Rho GAP arm as RhoA-specific and showed it is allosterically activated by direct binding of GTP-Rap to the RBD, with PI3K required in cells, establishing ARAP3 as a coincidence detector of Rap-GTP and PtdIns(3,4,5)P3.

    Evidence In vitro GAP and direct Rap-binding assays plus cellular PI3K inhibition

    PMID:15296756

    Open questions at the time
    • Structural interface of Rap-RBD binding not determined
    • How PtdIns(3,4,5)P3 and Rap inputs are integrated mechanistically unresolved
  3. 2004 High

    Identified Src-family kinase phosphorylation of C-terminal tyrosines Y1399/Y1404 as a negative regulatory input, since mutating these sites enhanced ARAP3 activity and adhesion-dependent inhibition of spreading.

    Evidence SFK co-expression, pharmacological inhibitors, site-directed mutagenesis, RhoA/Rac1 activity assays

    PMID:15546919

    Open questions at the time
    • Downstream effector of phosphorylated tyrosines not identified at this stage
    • In vivo relevance of phosphoregulation not tested
  4. 2004 Medium

    Implicated ARAP3 in membrane internalization by showing its loss impairs anthrax protective antigen entry, consistent with a vesicle-trafficking role.

    Evidence Genome-wide gene inactivation screen with antisense validation and toxin survival assay

    PMID:15569923

    Open questions at the time
    • Mechanistic link between ARAP3 GAP activity and toxin uptake not established
    • Single-lab phenotypic screen without enzymatic dissection
  5. 2006 High

    Demonstrated the cellular consequence of coordinated GTPase control: ARAP3 is required for growth-factor-induced lamellipodia, with its loss raising RhoA and Arf6 activity and mislocalizing Rac.

    Evidence RNAi in endothelial cells with RhoA/Arf6/Rac activity assays and confocal morphology

    PMID:16418224

    Open questions at the time
    • Did not separate Arf6 versus RhoA contributions to lamellipodia
    • Recruitment kinetics at PtdIns(3,4,5)P3 sites not measured
  6. 2007 High

    Revealed a protein-interaction layer by identifying a SAM-domain heterodimer between ARAP3 and the PtdIns(3,4,5)P3 phosphatase SHIP2, suggesting spatial coupling of lipid production and turnover.

    Evidence Yeast two-hybrid, endogenous reciprocal Co-IP, in vitro SAM binding

    PMID:17314030

    Open questions at the time
    • Functional consequence of the ARAP3-SHIP2 complex for signaling not tested
    • Stoichiometry and cellular context of the interaction unknown
  7. 2009 High

    Defined the unusual membrane-targeting mechanism, showing PtdIns(3,4,5)P3 binding requires cooperation of tandem PH domains, an N-terminal linker, and the SAM domain rather than a single PH module.

    Evidence Lipid-binding assays with truncations and point mutants

    PMID:19786092

    Open questions at the time
    • High-resolution structure of the bound state not yet available
    • Conflicts with later finding that PH1 alone suffices needed reconciling
  8. 2009 High

    Provided the structural basis for the SHIP2 interaction by solving the Arap3-SAM NMR structure and showing it uses a canonical SAM-SAM binding mode shared with EphA2.

    Evidence NMR solution structure, ITC, mutagenesis, modeling

    PMID:19765305

    Open questions at the time
    • Did not establish in vivo signaling output of the SAM heterodimer
    • Competition among SAM partners not addressed
  9. 2010 High

    Positioned ARAP3 genetically as the PI3Kα effector for angiogenesis by showing both knockout and a PtdIns(3,4,5)P3-uncoupling knock-in mouse cause endothelial-autonomous sprouting defects and mid-gestation lethality.

    Evidence Arap3 knockout and lipid-binding point-mutant knock-in mice with ex vivo explants and genetic epistasis

    PMID:20978237

    Open questions at the time
    • Relative in vivo contributions of Arf6 versus RhoA control not dissected
    • Downstream cytoskeletal effectors in sprouting not mapped
  10. 2010 Medium

    Extended the Rap1-effector role to neuronal differentiation, showing ARAP3 inactivates RhoA downstream of Rap1 to permit bFGF- and NGF-induced neurite outgrowth.

    Evidence Dominant-negative ARAP3 in PC12 cells with GTP-RhoA assays, Rap1-RhoA Co-IP, and neurite quantification

    PMID:20200473 PMID:20578246

    Open questions at the time
    • Relied on dominant-negative rather than loss-of-function
    • Endogenous ARAP3 requirement in neurons not confirmed
  11. 2010 Medium

    Linked ARAP3 to suppression of cancer cell invasion, showing overexpression inhibits gastric carcinoma peritoneal dissemination in a manner dependent on both the Rho GAP domain and the Src-target tyrosines.

    Evidence Overexpression with domain and tyrosine mutants in dissemination, adhesion, and invasion assays

    PMID:21076469

    Open questions at the time
    • Overexpression-based; endogenous tumor-suppressive role not tested
    • Connection to Arf6 cycling in invasion not examined
  12. 2011 High

    Defined a physiological immune role, showing ARAP3 acts downstream of Rap to keep neutrophils quiescent by restraining β2 integrin affinity and avidity.

    Evidence Conditional knockout neutrophils with integrin activation, flow, intravital, and chemotaxis assays

    PMID:21490342

    Open questions at the time
    • Did not separate which GAP activity controls integrin signaling
    • Molecular link from ARAP3 to inside-out signaling unmapped
  13. 2012 High

    Pinned the neutrophil phenotype to PI3K input by showing a PH-domain point-mutant knock-in (R302,303A) uncoupled from PtdIns(3,4,5)P3 recapitulates β2 integrin dysregulation and impaired recruitment in vivo.

    Evidence PH-domain point-mutant knock-in mouse with integrin assays, chemotaxis, peritonitis/arthritis models, bone marrow chimeras

    PMID:23180820

    Open questions at the time
    • Downstream GTPase events controlling integrin activation not resolved
    • Cell-intrinsic versus systemic effects only partly separated
  14. 2012 High

    Resolved the structural basis of phosphotyrosine readout, showing the Vav2 SH2 domain directly binds the Src-phosphorylated C-terminal tyrosines with micromolar affinity, identifying a recruited partner of inhibited ARAP3.

    Evidence ITC, NMR chemical shift perturbation, NMR structure of Vav2 SH2-pY1408 complex, in vivo Co-IP

    PMID:22750419

    Open questions at the time
    • Functional consequence of Vav2 recruitment to ARAP3 not established
    • Whether recruitment alters ARAP3 GAP output unknown
  15. 2012 Medium

    Characterized a second SAM-domain partner, defining the heterotypic Arap3-SAM/Odin-Sam1 interface and binding topology.

    Evidence NMR, SPR, ITC, molecular docking

    PMID:23239578

    Open questions at the time
    • Cellular and physiological role of the ARAP3-Odin complex untested
    • How Odin and SHIP2 compete for the same SAM domain unresolved
  16. 2013 Medium

    Broadened the vascular role to lymphatics, placing ARAP3 downstream of Vegfc as a mediator required for lymphangiogenesis in mouse and zebrafish.

    Evidence Mouse expression profiling, zebrafish functional analysis, in vitro Vegfc assays, in vivo lymphatic analysis

    PMID:24163130

    Open questions at the time
    • GTPase targets in lymphatic endothelium not dissected
    • Direct Vegfc-to-ARAP3 signaling link not biochemically defined
  17. 2016 High

    Explained RhoA substrate preference at atomic resolution by solving the RhoA-RhoGAP domain complex and identifying residues governing catalysis and specificity over Rac1 and Cdc42.

    Evidence X-ray crystallography, GTPase assays, ITC, mutagenesis

    PMID:27311713

    Open questions at the time
    • Did not capture the Rap-activated conformation
    • Full-length autoregulated state not structurally resolved
  18. 2023 High

    Refined the lipid-recognition model by showing PH1 alone is sufficient for specific PtdIns(3,4,5)P3 binding, solving apo and lipid-bound structures and tying PH1 binding to inhibition of breast cancer invasion.

    Evidence Liposome pull-down, SPR, NMR, crystallography of PH1, cell invasion assays with PH1 mutants

    PMID:36674645

    Open questions at the time
    • Relationship between PH1-only binding and earlier multi-domain requirement not fully reconciled
    • Structure of all five PH domains together unsolved
  19. 2024 High

    Established a barrier-protective function, showing ARAP3 limits microvascular permeability through both endothelial cells (restraining FPR1 and VE-cadherin internalization) and neutrophils (limiting NET formation).

    Evidence Arap3 knockout mouse, endothelial permeability assays, adoptive transfer, NET inhibition, influenza model

    PMID:38734878

    Open questions at the time
    • Direct GAP-substrate events controlling VE-cadherin trafficking not pinpointed
    • Mechanism connecting ARAP3 to FPR1 expression unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the multiple inputs (PtdIns(3,4,5)P3 binding, Rap-GTP, Src phosphorylation, SAM partners) are integrated to set the timing and magnitude of Arf6 versus RhoA inactivation at a given membrane site remains unresolved.
  • No full-length autoinhibited structure
  • Functional output of SHIP2, Odin, and Vav2 binding not mechanistically integrated
  • Quantitative model of dual-GAP coordination in vivo lacking

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098772 molecular function regulator activity 4 GO:0140096 catalytic activity, acting on a protein 4 GO:0008289 lipid binding 3 GO:0060089 molecular transducer activity 3
Localization
GO:0005886 plasma membrane 3
Pathway
R-HSA-162582 Signal Transduction 3 R-HSA-168256 Immune System 3 R-HSA-1266738 Developmental Biology 2
Partners
ANKS1AARF6INPPL1RAP1RHOASHIP2SRCVAV2

Evidence

Reading pass · 21 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2002 ARAP3 is a specific PtdIns(3,4,5)P3/PtdIns(3,4)P2-stimulated Arf6 GAP both in vitro and in vivo, and both its Arf GAP and Rho GAP domains cooperate in mediating PI3K-dependent rearrangements in cell cytoskeleton and cell shape. ARAP3 was identified by selective capture on phosphoinositide affinity matrices from leukocyte extracts and has five PH domains. Phosphoinositide affinity matrix capture, mass spectrometry identification, in vitro and in vivo GAP activity assays Molecular cell High 11804589
2004 ARAP3 functions as a RhoA-preferring Rho GAP (not other Rho family members) and is directly activated in vitro by GTP-bound Rap proteins binding to its Ras-binding domain (RBD). This activation is GTP-dependent and specific for Rap versus other Ras family members. PI3K activity was required for Rap-mediated activation in a cellular context, suggesting PtdIns(3,4,5)P3-dependent membrane translocation is required for subsequent Rap activation. In vitro GAP activity assays, direct binding assays with Rap proteins, cellular PI3K inhibition experiments Current biology : CB High 15296756
2004 ARAP3 is tyrosine phosphorylated by Src-family kinases (SFKs) upon adhesion to fibronectin, growth factor stimulation, and co-expression with SFKs. Adhesion-induced phosphorylation was suppressed by SFK and PI3K inhibitors. ARAP3 inhibits cell spreading in a RhoGAP-dependent manner, reducing active RhoA and Rac1 levels. Mutation of phosphorylation sites Y1399 and Y1404 enhanced ARAP3 activities, indicating negative regulation by phosphorylation on these tyrosines. Co-expression with SFKs, pharmacological inhibitors, dominant-negative mutants, inducible expression, RhoA/Rac1 activity assays, site-directed mutagenesis Journal of cell science High 15546919
2004 ARAP3 deficiency impairs entry of anthrax protective antigen (PA) and its bound toxigenic moieties into human and mouse cells, identifying ARAP3 as a host factor essential for cellular internalization of anthrax toxin, consistent with its role in membrane vesicle trafficking. EST-based genome-wide gene inactivation screen, antisense expression, cell survival assay after PA-dependent toxin treatment Proceedings of the National Academy of Sciences of the United States of America Medium 15569923
2006 ARAP3 is essential for lamellipodia formation after growth factor stimulation in endothelial cells. ARAP3-deficient cells show increased RhoA and Arf6 activities, are more rounded, display fine stress fibres, and cannot produce lamellipodia. Rac was activated but mislocalized in ARAP3-deficient cells, likely due to increased Arf6 activity. ARAP3 recruitment to sites of elevated PtdIns(3,4,5)P3 allows localized RhoA inactivation and Arf6 cycling. RNAi knockdown in endothelial cells, RhoA/Arf6/Rac activity assays, confocal microscopy of cell morphology and actin dynamics Journal of cell science High 16418224
2006 ARAP3's domain structure includes five PH domains, an Arf GAP domain, three ankyrin repeats, a Rho GAP domain, and a Ras association domain. It is a PtdIns(3,4,5)P3-dependent GAP for Arf6 in vitro and in vivo, and a Rap-GTP-activated RhoA GAP in vitro requiring direct interaction between ARAP3 and Rap-GTP; in vivo, PtdIns(3,4,5)P3 is required to enable RhoA GAP activation by Rap-GTP. Protein purification, in vitro GAP activity assays, overexpression phenotype analysis in PAE cells Methods in enzymology High 16472652
2007 ARAP3 interacts with the PI(3,4,5)P3 phosphatase SHIP2 through a SAM domain-mediated heterodimeric interaction. The SAM domain of ARAP3 and the SAM domain of SHIP2 show specificity for heterodimeric interaction in vitro. This interaction was confirmed with endogenous proteins. Yeast two-hybrid screen, endogenous co-immunoprecipitation, in vitro SAM domain binding assay Cellular signalling High 17314030
2009 ARAP3 binds PtdIns(3,4,5)P3 through an unusual mechanism requiring the N-terminal tandem PH domains plus an N-terminal linker region. No single PH domain is sufficient for binding. The N-terminal SAM domain further contributes to substantial binding. Site-directed mutagenesis of either N-terminal PH domain greatly reduces PtdIns(3,4,5)P3 binding, and deletion of any single PH domain abolishes binding. PtdIns(3,4,5)P3 binding assays with truncation and point mutants, site-directed mutagenesis Cellular signalling High 19786092
2009 The NMR solution structure of Arap3-SAM was determined, and heterodimeric interaction with Ship2-SAM was characterized. Arap3-SAM associates with Ship2-SAM using a binding mode common to other SAM domain pairs, identical to Ship2-SAM/EphA2-SAM interaction. Key structural features mediating SAM-SAM interactions were identified. NMR solution structure determination, ITC, mutagenesis, molecular modeling BMC structural biology High 19765305
2010 ARAP3 deletion in mice causes embryonic death in mid-gestation due to an endothelial cell-autonomous defect in sprouting angiogenesis. Knock-in mice with an ARAP3 point mutant that cannot be activated by PtdIns(3,4,5)P3 have similar angiogenesis defects, establishing that PI3Kα signals through ARAP3 (via PtdIns(3,4,5)P3 activation) to control RhoA and Arf6 during angiogenesis. Arap3 knockout mouse, PtdIns(3,4,5)P3-binding point mutant knock-in mouse, ex vivo explant assays, genetic epistasis Science signaling High 20978237
2010 ARAP3 inactivates RhoA downstream of Rap1 during neurite outgrowth in PC12 cells in response to bFGF. Dominant-negative ARAP3 and dominant-negative Rap1 both reduced neurite formation, placing ARAP3 as a Rap1 effector that inactivates RhoA to enable neurite outgrowth. Dominant-negative ARAP3 expression in PC12 cells, GTP-RhoA activity assays, neurite outgrowth quantification Journal of cellular physiology Medium 20578246
2010 In PC12 cells responding to NGF, ARAP3 acts downstream of Rap1 to inactivate RhoA and enable neurite outgrowth. Dominant-negative ARAP3 prevented RhoA inactivation and abolished neurite formation. RhoA was co-immunoprecipitated with Rap1, and NGF activated Rap1. Dominant-negative expression, GTP-RhoA activity assays, co-immunoprecipitation of RhoA and Rap1, neurite outgrowth quantification Experimental & molecular medicine Medium 20200473
2010 ARAP3 overexpression in scirrhous gastric carcinoma cells inhibits peritoneal dissemination by regulating cell attachment to ECM and invasion. These effects required a functional Rho-GAP domain and the C-terminal tyrosine residues (Y1399/Y1404) phosphorylated by Src, but were suppressed by mutations in either the RhoGAP domain or these tyrosines. Overexpression in cancer cell lines, peritoneal dissemination assay, cell adhesion and invasion assays, RhoGAP domain mutants and tyrosine phosphorylation site mutants Oncogene Medium 21076469
2011 ARAP3 functions downstream of Rap in neutrophils to modulate β2 integrin affinity and avidity. ARAP3-deficient neutrophils are preactivated, show increased β2 integrin inside-out signaling, hyperresponsive adhesion-dependent functions (ROS formation, adhesion, spreading, granule release), and defective integrin-dependent chemotaxis. ARAP3 guards neutrophils in their quiescent state. Arap3 conditional knockout mouse neutrophils, β2 integrin activation assays, flow assays, intravital microscopy, in vitro chemotaxis Blood High 21490342
2012 PI3K regulates β2 integrin activity in neutrophils specifically through its effector ARAP3: neutrophils from ARAP3 PH domain point mutant knock-in mice (R302,303A, uncoupled from PI3K activation) show increased β2 integrin inside-out signaling and disturbed adhesion-dependent responses, with reduced neutrophil recruitment in vivo. Neutrophil chemotaxis was also affected. ARAP3 PH domain point mutant knock-in mouse, β2 integrin activation assays, in vitro chemotaxis, in vivo peritonitis and arthritis models, bone marrow chimeras Journal of immunology High 23180820
2012 Arap3-SAM interacts with the first SAM domain of Odin (Odin-Sam1) with low micromolar affinity. NMR, SPR, ITC, and molecular docking revealed a heterotypic SAM-SAM binding topology common to other SAM domain complexes, identifying structural determinants for the interaction. NMR spectroscopy, SPR, ITC, molecular docking Chembiochem Medium 23239578
2012 Vav2 SH2 domain interacts directly with phosphorylated Y1403 and Y1408 (corresponding to the Src-phosphorylated tyrosines) within the C-terminal region of Arap3, with dissociation constants of ~0.27 and ~1.40 μM respectively. The solution structures of Vav2 SH2 domain free and in complex with pY1408 peptide were determined, revealing the structural basis for this recognition. ITC, NMR chemical shift perturbation, NMR solution structure determination, Co-IP in vivo Journal of structural biology High 22750419
2013 ARAP3 is necessary for lymphatic vascular development in mice and zebrafish and acts as a mediator of the cellular response to Vegfc signaling in lymphatic endothelial cells. ARAP3 is downregulated in HLT mouse aberrant dermal lymphatic vessels, positioning it downstream of Vegfc in lymphangiogenesis. Mouse model gene expression profiling, zebrafish functional analysis, in vitro Vegfc signaling assays, in vivo lymphatic vessel analysis Human molecular genetics Medium 24163130
2016 Crystal structure of RhoA in complex with the RhoGAP domain of ARAP3 was solved, revealing the molecular interface. In vitro GTPase activity assays and ITC experiments identified crucial residues affecting RhoGAP catalytic activity and substrate specificity, explaining why ARAP3 preferentially activates RhoA over Rac1 and Cdc42. X-ray crystallography, in vitro GTPase activity assays, ITC, mutagenesis The Journal of biological chemistry High 27311713
2023 The first PH domain of Arap3 (PH1) is sufficient to interact with PI(3,4,5)P3 (and with lower affinity PI(4,5)P2). The crystal structure of Arap3-PH1 in apo form and in complex with diC4-PI(3,4,5)P3 was determined, revealing the structural basis for specific phosphoinositide recognition. PI(3,4,5)P3-binding by PH1 is essential for ARAP3's ability to inhibit breast cancer cell invasion. Liposome pull-down, SPR, NMR, X-ray crystallography of apo and PI(3,4,5)P3-bound PH1, cell invasion assays with PH1 mutants International journal of molecular sciences High 36674645
2024 ARAP3 protects against formylated peptide-induced microvascular permeability through both endothelial cells and neutrophils. In vitro, Arap3-/- endothelial monolayers show enhanced permeability due to upregulated FPR1 and enhanced VE-cadherin internalisation. In vivo, loss of ARAP3 leads to excessive microvascular leakage and neutrophil extracellular trap (NET) formation; pharmacological inhibition of NET formation abrogated the excessive leakage. Arap3 knockout mouse, endothelial monolayer permeability assays, adoptive transfer experiments, pharmacological NET inhibition, bronchoalveolar lavage analysis, influenza infection model The Journal of pathology High 38734878

Source papers

Stage 0 corpus · 27 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2002 Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho GTPases, by selective capture on phosphoinositide affinity matrices. Molecular cell 245 11804589
2004 ARAP3 is a PI3K- and rap-regulated GAP for RhoA. Current biology : CB 104 15296756
2004 ARAP3 is transiently tyrosine phosphorylated in cells attaching to fibronectin and inhibits cell spreading in a RhoGAP-dependent manner. Journal of cell science 51 15546919
2007 The PI3K effector Arap3 interacts with the PI(3,4,5)P3 phosphatase SHIP2 in a SAM domain-dependent manner. Cellular signalling 46 17314030
2006 ARAP3 is essential for formation of lamellipodia after growth factor stimulation. Journal of cell science 46 16418224
2011 The GTPase-activating protein ARAP3 regulates chemotaxis and adhesion-dependent processes in neutrophils. Blood 44 21490342
2010 PI3K signaling through the dual GTPase-activating protein ARAP3 is essential for developmental angiogenesis. Science signaling 39 20978237
2010 The RGM protein DRAG-1 positively regulates a BMP-like signaling pathway in Caenorhabditis elegans. Development (Cambridge, England) 38 20534671
2010 Neurite outgrowth from PC12 cells by basic fibroblast growth factor (bFGF) is mediated by RhoA inactivation through p190RhoGAP and ARAP3. Journal of cellular physiology 35 20578246
2004 EST-based genome-wide gene inactivation identifies ARAP3 as a host protein affecting cellular susceptibility to anthrax toxin. Proceedings of the National Academy of Sciences of the United States of America 34 15569923
2010 p190RhoGAP and Rap-dependent RhoGAP (ARAP3) inactivate RhoA in response to nerve growth factor leading to neurite outgrowth from PC12 cells. Experimental & molecular medicine 32 20200473
2013 The neogenin/DCC homolog UNC-40 promotes BMP signaling via the RGM protein DRAG-1 in C. elegans. Development (Cambridge, England) 29 24004951
2013 Arap3 is dysregulated in a mouse model of hypotrichosis-lymphedema-telangiectasia and regulates lymphatic vascular development. Human molecular genetics 29 24163130
2009 The Sam domain of the lipid phosphatase Ship2 adopts a common model to interact with Arap3-Sam and EphA2-Sam. BMC structural biology 29 19765305
2010 ARAP3 inhibits peritoneal dissemination of scirrhous gastric carcinoma cells by regulating cell adhesion and invasion. Oncogene 25 21076469
2012 Phosphoinositide 3-OH kinase regulates integrin-dependent processes in neutrophils by signaling through its effector ARAP3. Journal of immunology (Baltimore, Md. : 1950) 18 23180820
2012 Heterotypic Sam-Sam association between Odin-Sam1 and Arap3-Sam: binding affinity and structural insights. Chembiochem : a European journal of chemical biology 17 23239578
2009 ARAP3 binding to phosphatidylinositol-(3,4,5)-trisphosphate depends on N-terminal tandem PH domains and adjacent sequences. Cellular signalling 14 19786092
2016 Structural Basis for the Specific Recognition of RhoA by the Dual GTPase-activating Protein ARAP3. The Journal of biological chemistry 11 27311713
2016 Next-generation sequence detects ARAP3 as a novel oncogene in papillary thyroid carcinoma. OncoTargets and therapy 11 27920554
2012 Identification and structural basis for a novel interaction between Vav2 and Arap3. Journal of structural biology 10 22750419
2006 Purification of ARAP3 and characterization of GAP activities. Methods in enzymology 6 16472652
2014 ARAP3 functions in hematopoietic stem cells. PloS one 3 25542002
2024 ARAP3 protects from excessive formylated peptide-induced microvascular leakage by acting on endothelial cells and neutrophils. The Journal of pathology 2 38734878
2023 Structural Insights Uncover the Specific Phosphoinositide Recognition by the PH1 Domain of Arap3. International journal of molecular sciences 1 36674645
2023 Genetic Variants in Genes Correlated to the PI3K/AKT Pathway: The Role of ARAP3, CDH5, KIF11 and RELN in Primary Lymphedema. Lymphology 1 39207407
2020 Mutations in the ARAP3 Gene in Three Families with Primary Lymphedema Negative for Mutations in Known Lymphedema-Associated Genes. International journal of genomics 0 32908855

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