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

ADP-ribosylation factor GTPase activating protein 2

ArfGAP2
Top mentioned proteins: COPI, GAP, ARF1, ARF GAP, p16
Papers on ArfGAP2
Activation of Gαi at the Golgi by GIV/Girdin imposes finiteness in Arf1 signaling.
New
Ghosh et al., San Diego, United States. In Dev Cell, May 2015
Several interactions with other major components of Golgi trafficking-e.g., active Arf1, its regulator, ArfGAP2/3, and the adaptor protein β-COP-enable GIV to coordinately regulate Arf1 signaling.
The ArfGAP2/3 Glo3 and ergosterol collaborate in transport of a subset of cargoes.
Spang et al., Basel, Switzerland. In Biol Open, 2014
Here we show that a subset of cargoes depends on the ArfGAP2/3 Glo3 and ergosterol to maintain their proper localization at the plasma membrane.
ArfGAP3 regulates the transport of cation-independent mannose 6-phosphate receptor in the post-Golgi compartment.
Randazzo et al., Bethesda, United States. In Curr Biol, 2013
The effect was specific for ArfGAP3 and dependent on its GAP activity, because the phenotype was rescued by ArfGAP3 but not by ArfGAP1, ArfGAP2, or the GAP domain mutants of ArfGAP3.
Selection of new appropriate reference genes for RT-qPCR analysis via transcriptome sequencing of cynomolgus monkeys (Macaca fascicularis).
Chang et al., South Korea. In Plos One, 2012
Combined analysis by these 3 programs showed that ADP-ribosylation factor GTPase activating protein 2 (ARFGAP2), morf4 family associated protein 1 (MRFAP1), and ADP-ribosylation factor-like 1 (ARL1) are the most appropriate reference genes for accurate normalization.
Distinct role of subcomplexes of the COPI coat in the regulation of ArfGAP2 activity.
GeneRIF
Cassel et al., Haifa, Israel. In Traffic, 2012
analysis of the distinct role of subcomplexes of the COPI coat in the regulation of ArfGAP2 activity
Identification of a high-affinity network of secretagogin-binding proteins involved in vesicle secretion.
Linse et al., Lund, Sweden. In Mol Biosyst, 2011
Here, the cellular interaction network of secretagogin has been expanded with nine proteins: SNAP-23, DOC2alpha, ARFGAP2, rootletin, KIF5B, β-tubulin, DDAH-2, ATP-synthase and myeloid leukemia factor 2, based on screening of a high content protein array and validation and quantification of binding with surface plasmon resonance and GST pulldown assays.
Protein networks involved in vesicle fusion, transport, and storage revealed by array-based proteomics.
O'Connell et al., Lund, Sweden. In Methods Mol Biol, 2010
Six of the novel target proteins have important roles in vesicle trafficking; SNAP-23, ARFGAP2, and DOC2alpha are involved in regulating fusion of vesicles to membranes, kinesin 5B and tubulin are essential for transport of vesicles in the cell, and rootletin builds up the rootlet, which is believed to function as scaffold for vesicles.
ARFGAP2 and ARFGAP3 are essential for COPI coat assembly on the Golgi membrane of living cells.
GeneRIF
Presley et al., Göteborg, Sweden. In J Biol Chem, 2010
ARFGAP2 and ARFGAP3 are essential for COPI coat assembly on the Golgi membrane of living cells.
Arf GAPs: gatekeepers of vesicle generation.
Review
Randazzo et al., Basel, Switzerland. In Febs Lett, 2010
In this review, we will focus mainly on the Arf GAPs that play a role in vesicle formation, Arf GAP1, Arf GAP2 and Arf GAP3 and their yeast homologues, Gcs1p and Glo3p.
The GAP domain and the SNARE, coatomer and cargo interaction region of the ArfGAP2/3 Glo3 are sufficient for Glo3 function.
Spang et al., Basel, Switzerland. In Traffic, 2009
Our data suggest that membrane-interaction modules and cargo-sensing regions have evolved independently in ArfGAP1s versus ArfGAP2/3s.
Arf GAP2 is positively regulated by coatomer and cargo.
Randazzo et al., Bethesda, United States. In Cell Signal, 2009
Arf GAP2 is one of four Arf GAPs that function in the Golgi apparatus.
Three homologous ArfGAPs participate in coat protein I-mediated transport.
GeneRIF
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.
Discrete determinants in ArfGAP2/3 conferring Golgi localization and regulation by the COPI coat.
Cassel et al., Haifa, Israel. In Mol Biol Cell, 2009
From yeast to mammals, two types of GTPase-activating proteins, ArfGAP1 and ArfGAP2/3, control guanosine triphosphate (GTP) hydrolysis on the small G protein ADP-ribosylation factor (Arf) 1 at the Golgi apparatus.
Differential roles of ArfGAP1, ArfGAP2, and ArfGAP3 in COPI trafficking.
GeneRIF
Wieland et al., Heidelberg, Germany. In J Cell Biol, 2008
Differential roles of ArfGAP1, ArfGAP2, and ArfGAP3 in COPI trafficking
Two human ARFGAPs associated with COP-I-coated vesicles.
GeneRIF
Duden et al., Cambridge, United Kingdom. In Traffic, 2007
human ARFGAP2 and ARFGAP3 are associated with COP-I-coated vesicles and function in COP I traffic
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