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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

ADP-ribosylation factor GTPase activating protein 1

ARF GAP, ARFGAP1, ADP-ribosylation factor GTPase-activating protein, GAP protein
The protein encoded by this gene is a GTPase-activating protein (GAP) which associates with the Golgi apparatus and which interacts with ADP-ribosylation factor 1 (ARF1). The encoded protein promotes hydrolysis of ARF1-bound GTP and is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles. Dissociation of the coat proteins is required for the fusion of these vesicles with target compartments. The activity of this protein is stimulated by phosphoinosides and inhibited by phosphatidylcholine. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: GAP, p16, ARF1, Actin, CAN
Papers using ARF GAP antibodies
The GGAs Promote ARF-Dependent Recruitment of Clathrin to the TGN.
Hotchin Neil, In PLoS ONE, 2000
... Green fluorescent fusion proteins were made by inserting various fragments of ARFGAP1 cDNA into the expression plasmid pEGFP-C3 (Clontech).
Papers on ARF GAP
Structural basis for the binding of tryptophan-based motifs by δ-COP.
Owen et al., Cambridge, United Kingdom. In Proc Natl Acad Sci U S A, Dec 2015
Mutations designed on the basis of the structure in conjunction with isothermal titration calorimetry confirm the mode of binding and show that mammalian δ-COP binds related tryptophan-based motifs such as that from ArfGAP1 in a similar manner.
A PH Domain with Dual Phospholipid Binding Sites Regulates the ARF GAP, ASAP1.
Lambright et al., Atlanta, United States. In Structure, Dec 2015
(2015) report the crystal structures of the apo- and dibutyryl-PI(4,5)P2 bound forms of the PH domain from the ARF GAP, ASAP1.
Gravitropism in Arabidopsis thaliana: Root-specific action of the EHB gene and violation of the resultant law.
Galland et al., Marburg an der Lahn, Germany. In J Plant Physiol, Oct 2015
A tropism mutant lacking the EHB1 protein, which interacts with ARF-GAP (ARF GTPase-activating protein) and thus indirectly with a small ARF-type G protein, displayed a lower gravitropic threshold for roots and also enhanced bending, while the responses of the hypocotyls remained nearly unaffected.
Basolateral Endocytic Recycling Requires RAB-10 and AMPH-1 Mediated Recruitment of RAB-5 GAP TBC-2 to Endosomes.
Grant et al., United States. In Plos Genet, Sep 2015
Here we focused on the recycling function of the early endosome and the regulation of RAB-5 by GAP protein TBC-2 in the basolateral C. elegans intestine.
Identification of Atg2 and ArfGAP1 as Candidate Genetic Modifiers of the Eye Pigmentation Phenotype of Adaptor Protein-3 (AP-3) Mutants in Drosophila melanogaster.
Dell'Angelica et al., Los Angeles, United States. In Plos One, 2014
The second critical region included the ArfGAP1 gene, which encodes a conserved GTPase-activating protein with specificity towards GTPases of the Arf family.
Interaction of LRRK2 with kinase and GTPase signaling cascades.
Wolozin et al., Boston, United States. In Front Mol Neurosci, 2013
Binding to GTPases, GTPase-activating proteins and GTPase exchange factors are another strong theme in LRRK2 biology, with LRRK2 binding to rac1, cdc42, rab5, rab7L1, endoA, RGS2, ArfGAP1, and ArhGEF7.
Chemosensory signaling controls motility and subcellular polarity in Myxococcus xanthus.
Zusman et al., Berkeley, United States. In Curr Opin Microbiol, 2012
The Frz signal is mediated by a GTPase/GAP protein pair that establishes cell polarity and directs the motility systems.
ArfGAP1 function in COPI mediated membrane traffic: currently debated models and comparison to other coat-binding ArfGAPs.
Randazzo et al., Bethesda, United States. In Histol Histopathol, 2012
The ArfGAPs are a family of proteins containing an ArfGAP catalytic domain that induces the hydrolysis of GTP bound to the small guanine nucleotide binding-protein ADP-ribosylation factor (Arf).
Molecular therapies for tuberous sclerosis and neurofibromatosis.
Weiss et al., Cincinnati, United States. In Curr Neurol Neurosci Rep, 2012
Their protein products, hamartin and tuberin, respectively, form a dimer that acts via the GAP protein Rheb (Ras homolog enhanced in brain) to directly inhibit mTOR, again resulting in upregulation.
ARFGAP3, an androgen target gene, promotes prostate cancer cell proliferation and migration.
Inoue et al., Tokyo, Japan. In Int J Cancer, 2012
our results suggest that ARFGAP3 is a novel androgen-regulated gene that can promote prostate cancer cell proliferation and migration in collaboration with paxillin.
ArfGAP1 is a GTPase activating protein for LRRK2: reciprocal regulation of ArfGAP1 by LRRK2.
Dawson et al., Baltimore, United States. In J Neurosci, 2012
ArfGAP1 is identified as the first GTPase activating protein (GAP) for leucine-rich repeat kinase 2 (LRRK2).
ARFGAP1 promotes AP-2-dependent endocytosis.
Hsu et al., Boston, United States. In Nat Cell Biol, 2011
role of ARFGAP1 in AP-2-regulated endocytosis has mechanistic parallels with its roles in COPI transport, as both its GAP activity and coat function contribute to promoting AP-2 transport
Arf GAPs: gatekeepers of vesicle generation.
Randazzo et al., Basel, Switzerland. In Febs Lett, 2010
Arf GAP proteins are a versatile and diverse group of proteins.
ArfGAP1 interacts with coat proteins through tryptophan-based motifs.
Cassel et al., Haifa, Israel. In Biochem Biophys Res Commun, 2010
these findings point to mechanistic differences between ArfGAP1 and the other ArfGAPs known to function in the COPI system.
Three homologous ArfGAPs participate in coat protein I-mediated transport.
Nakayama et al., Kyoto, Japan. In J Biol Chem, 2009
ArfGAP1, ArfGAP2, and ArfGAP3 have overlapping roles in regulating COPI function in Golgi-to-ER retrograde transport.
Asymmetric tethering of flat and curved lipid membranes by a golgin.
Antonny et al., Antibes, France. In Science, 2008
This asymmetric tethering relied on motifs that sensed membrane curvature both in the N terminus of GMAP-210 and in ArfGAP1, which controlled the interaction of the C terminus of GMAP-210 with the small guanine nucleotide-binding protein Arf1.
Key components of the fission machinery are interchangeable.
Hsu et al., Boston, United States. In Nat Cell Biol, 2006
Here, we show that ARFGAP1, a GTPase-activating protein (GAP) for ADP-ribosylation factor 1 (ARF1), couples to either BARS or endophilin B for vesicle formation by the coat protein I (COPI) complex - a finding that reveals an unanticipated mechanistic flexibility in mammalian COPI transport.
An alpha4 integrin-paxillin-Arf-GAP complex restricts Rac activation to the leading edge of migrating cells.
Ginsberg et al., San Diego, United States. In Nat Cell Biol, 2005
The paxillin LD4 domain mediates this reduction in Rac activity by recruiting an ADP-ribosylation factor GTPase-activating protein (Arf-GAP) that decreases Arf activity, thereby inhibiting Rac.
Mouse model of Noonan syndrome reveals cell type- and gene dosage-dependent effects of Ptpn11 mutation.
Neel et al., Boston, United States. In Nat Med, 2004
Severely affected Ptpn11(D61G/+) embryos ( approximately 50%) have multiple cardiac defects similar to those in mice lacking the Ras-GAP protein neurofibromin.
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