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ArfGAP with RhoGAP domain, ankyrin repeat and PH domain 3

ARAP3, Centd3, PtdIns(3,4,5)P3-binding protein
This gene encodes a phosphoinositide binding protein containing ARF-GAP, RHO-GAP, RAS-associating, and pleckstrin homology domains. The ARF-GAP and RHO-GAP domains cooperate in mediating rearrangements in the cell cytoskeleton and cell shape. It is a specific PtdIns(3,4,5)P3/PtdIns(3,4)P2-stimulated Arf6-GAP protein. An alternatively spliced transcript has been found for this gene, but its biological validity has not been determined. [provided by RefSeq, Sep 2008] (from NCBI)
Top mentioned proteins: GAP, RhoA, PI3K, p16, Rhodopsin
Papers on ARAP3
An Islet-Targeted Genome-Wide Association Scan Identifies Novel Genes Implicated in Cytokine-Mediated Islet Stress in Type 2 Diabetes.
Nunemaker et al., Torrance, United States. In Endocrinology, Sep 2015
Significant evidence of association was found between AIRg and single nucleotide polymorphisms in Arap3 (5q31.3),
NEDD9/Arf6-dependent endocytic trafficking of matrix metalloproteinase 14: a novel mechanism for blocking mesenchymal cell invasion and metastasis of breast cancer.
Pugacheva et al., Morgantown, United States. In Oncogene, Jul 2015
NEDD9 directly binds to Arf6-GTPase-activating protein, ARAP3 and Arf6-effector GGA3, thereby facilitating the Arf6 inactivation required for MMP14/TIMP2 targeting to late endosomes.
The Arf GTPase-activating protein family is exploited by Salmonella enterica serovar Typhimurium to invade nonphagocytic host cells.
Koronakis et al., Cambridge, United Kingdom. In Mbio, 2014
The Arf6 GAPs ACAP1 and ADAP1 and the Arf1 GAP ASAP1 localized at Salmonella-induced ruffles, which was not the case for the plasma membrane-localized Arf6 GAPs ARAP3 and GIT1 or the Golgi-associated Arf1 GAP1.
Identification of specific gene modules in mouse lung tissue exposed to cigarette smoke.
Meng et al., Tianjin, China. In Asian Pac J Cancer Prev, 2014
Seven hub genes were identified as well, including Fip1l1, Anp32a, Acsl4, Evl, Sdc1, Arap3 and Cd52.
CD and NMR conformational studies of a peptide encompassing the Mid Loop interface of Ship2-Sam.
Leone et al., Napoli, Italy. In Biopolymers, 2014
The Sam domain of Ship2 (Ship2-Sam) binds to the Sam domains of the EphA2 receptor (EphA2-Sam) and the PI3K effector protein Arap3 (Arap3-Sam).
Arap3 is dysregulated in a mouse model of hypotrichosis-lymphedema-telangiectasia and regulates lymphatic vascular development.
Hogan et al., Australia. In Hum Mol Genet, 2014
Expression studies and functional analysis in zebrafish and mice revealed one candidate, ArfGAP with RhoGAP domain, Ankyrin repeat and PH domain 3 (ARAP3), which is down-regulated in HLT mouse lymphatic vessels and necessary for lymphatic vascular development in mice and zebrafish.
Integrin-matrix clusters form podosome-like adhesions in the absence of traction forces.
Sheetz et al., Singapore, Singapore. In Cell Rep, 2014
Enrichment of PIP3 precedes N-WASP activation and the recruitment of RhoA-GAP ARAP3.
Whole genome sequence analysis suggests intratumoral heterogeneity in dissemination of breast cancer to lymph nodes.
Shaw et al., Leicester, United Kingdom. In Plos One, 2013
We also identified dominant clonal variants that progressed from tumor to node, including SNVs in TP53 and ARAP3, which mediates rearrangements to the cytoskeleton and cell shape, and an insertion in TOP2A, the expression of which is significantly associated with tumor proliferation and can segregate breast cancers by outcome.
ARAP3 functions in hematopoietic stem cells.
Tong et al., Philadelphia, United States. In Plos One, 2013
ARAP3 is a GTPase-activating protein (GAP) that inactivates Arf6 and RhoA small GTPases.
Small GTPase Rap1 regulates cell migration through regulation of small GTPase RhoA activity in response to transforming growth factor-β1.
Park et al., Ch'unch'ŏn, South Korea. In J Cell Physiol, 2013
Furthermore, si-RNA of ARAP3 (Rap-dependent RhoGAP) increased GTP-RhoA level and cell migration.
Heterotypic Sam-Sam association between Odin-Sam1 and Arap3-Sam: binding affinity and structural insights.
Leone et al., Napoli, Italy. In Chembiochem, 2013
Arap3 is a phosphatidylinositol 3 kinase effector protein that plays a role as GTPase activator (GAP) for Arf6 and RhoA.
Phosphoinositide 3-OH kinase regulates integrin-dependent processes in neutrophils by signaling through its effector ARAP3.
Vermeren et al., Cambridge, United Kingdom. In J Immunol, 2013
ARAP3, a GTPase activating protein for Rho and Arf family GTPases, is one of many phosphoinositide 3-OH kinase (PI3K) effectors.
Targeting the junction of CɛmX and ɛ-migis for the specific depletion of mIgE-expressing B cells.
Wu et al., Gaithersburg, United States. In Mol Immunol, 2012
Our results indicate that antibodies obtained from our phage library that target ɛ-migis bind to a variety of human cells irrespective of mIgE expression, possibly due to homology between ɛ-migis and a region of phosphoinositide-binding protein (ARAP3).
Identification and structural basis for a novel interaction between Vav2 and Arap3.
Shi et al., Hefei, China. In J Struct Biol, 2012
In this study, Arap3, a dual GTPase-activating protein (GAP) for RhoA and Arf6, was first identified to be a novel interaction partner for Vav2 both in vitro and in vivo.
Exchange protein activated by cyclic adenosine monophosphate regulates the switch between adipogenesis and osteogenesis of human mesenchymal stem cells through increasing the activation of phosphatidylinositol 3-kinase.
Tong et al., Hangzhou, China. In Int J Biochem Cell Biol, 2012
Inhibition of PI3K by a specific inhibitor or inhibition of Arf and Rho GAP adapter protein 3 (ARAP3, a phosphatidylinositol (PtdIns)(3,4,5)P(3) binding protein) by ARAP3 siRNA led to the recovery of RhoA and FAK activities.
The GTPase-activating protein ARAP3 regulates chemotaxis and adhesion-dependent processes in neutrophils.
Vermeren et al., Cambridge, United Kingdom. In Blood, 2011
We report here the first characterization of the role of ARAP3 in murine neutrophils
ARAP3 inhibits peritoneal dissemination of scirrhous gastric carcinoma cells by regulating cell adhesion and invasion.
Sakai et al., Tokyo, Japan. In Oncogene, 2011
ARAP3 is a unique Src substrate that suppresses peritoneal dissemination of scirrhous gastric carcinoma cells.
ARAP3 binding to phosphatidylinositol-(3,4,5)-trisphosphate depends on N-terminal tandem PH domains and adjacent sequences.
Vermeren et al., Cambridge, United Kingdom. In Cell Signal, 2010
None of the individual PH domains can bind to PtdIns(3,4,5)P3; rather, a fragment comprising two PH domains and an N-terminal linker is minimally required for binding.
PI3K signaling through the dual GTPase-activating protein ARAP3 is essential for developmental angiogenesis.
Vermeren et al., Cambridge, United Kingdom. In Sci Signal, 2009
PI3K signaling through the dual GTPase-activating protein ARAP3 is essential for developmental angiogenesis.
Nck adapters are involved in the formation of dorsal ruffles, cell migration, and Rho signaling downstream of the platelet-derived growth factor beta receptor.
Aspenström et al., Uppsala, Sweden. In J Biol Chem, 2008
the Nck adapters are needed for signaling to Rho GTPases and actin dynamics downstream of the PDGFbeta receptor
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