A new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an ADP-ribosylation factor GTPase-activating protein activity, is involved in paxillin recruitment to focal adhesions and cell migration

A new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an ADP-ribosylation factor GTPase-activating protein activity, is involved in paxillin recruitment to focal adhesions and cell migration

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http://www.wikidata.org/entity/Q24548827

Q24548827

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RNF5, a RING finger protein that regulates cell motility by targeting paxillin ubiquitination and altered localization Identification of a link between the SAMP repeats of adenomatous polyposis coli tumor suppressor and the Src homology 3 domain of DDEF The Q-soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor (Q-SNARE) SNAP-47 Regulates Trafficking of Selected Vesicle-associated Membrane Proteins (VAMPs).Paxillin-dependent paxillin kinase linker and p21-activated kinase localization to focal adhesions involves a multistep activation pathway The association of ASAP1, an ADP ribosylation factor-GTPase activating protein, with focal adhesion kinase contributes to the process of focal adhesion assembly Coupling of PAK-interacting exchange factor PIX to GIT1 promotes focal complex disassembly Expression of AMAP1, an ArfGAP, provides novel targets to inhibit breast cancer invasive activities Regulation of Bin1 SH3 domain binding by phosphoinositides An ADP-ribosylation factor GTPase-activating protein Git2-short/KIAA0148 is involved in subcellular localization of paxillin and actin cytoskeletal organization PAG3/Papalpha/KIAA0400, a GTPase-activating protein for ADP-ribosylation factor (ARF), regulates ARF6 in Fcgamma receptor-mediated phagocytosis of macrophages ACAPs are arf6 GTPase-activating proteins that function in the cell periphery Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion Identification and characterization of a novel Pyk2/related adhesion focal tyrosine kinase-associated protein that inhibits alpha-synuclein phosphorylation Temporal regulation of EGF signalling networks by the scaffold protein Shc1 A novel muscle LIM-only protein is generated from the paxillin gene locus in Drosophila EPB41L5 functions to post-transcriptionally regulate cadherin and integrin during epithelial-mesenchymal transition Selenoprotein K regulation of palmitoylation and calpain cleavage of ASAP2 is required for efficient FcγR-mediated phagocytosis.SH3 domain-based phototrapping in living cells reveals Rho family GAP signaling complexes Interaction of POB1, a downstream molecule of small G protein Ral, with PAG2, a paxillin-binding protein, is involved in cell migration.Paxillin: a focal adhesion-associated adaptor protein.The LD4 motif of paxillin regulates cell spreading and motility through an interaction with paxillin kinase linker (PKL).Substrate specificities and activities of AZAP family Arf GAPs in vivo.Dynamic motion of paxillin on actin filaments in living endothelial cells Myoblasts and macrophages share molecular components that contribute to cell-cell fusion Interaction of paxillin with p21-activated Kinase (PAK). Association of paxillin alpha with the kinase-inactive and the Cdc42-activated forms of PAK3.Thrombospondin type I domain containing 7A (THSD7A) mediates endothelial cell migration and tube formation.Requirement for Arf6 in breast cancer invasive activities.Cytohesin-2/ARNO, through its interaction with focal adhesion adaptor protein paxillin, regulates preadipocyte migration via the downstream activation of Arf6.Paxillin associates with poly(A)-binding protein 1 at the dense endoplasmic reticulum and the leading edge of migrating cells.DEF-1/ASAP1 is a GTPase-activating protein (GAP) for ARF1 that enhances cell motility through a GAP-dependent mechanism.Cell migration: GAPs between membrane traffic and the cytoskeleton.A novel mode of action of an ArfGAP, AMAP2/PAG3/Papa lpha, in Arf6 function.Constitutive p21-activated kinase (PAK) activation in breast cancer cells as a result of mislocalization of PAK to focal adhesions Molecular aspects of the cellular activities of ADP-ribosylation factors.ARF6: a newly appreciated player in G protein-coupled receptor desensitization.Comprehensive exploration of novel chimeric transcripts in clear cell renal cell carcinomas using whole transcriptome analysis Crk associates with a multimolecular Paxillin/GIT2/beta-PIX complex and promotes Rac-dependent relocalization of Paxillin to focal contacts Paxillin alpha and Crk-associated substrate exert opposing effects on cell migration and contact inhibition of growth through tyrosine phosphorylation GIT1 utilizes a focal adhesion targeting-homology domain to bind paxillin Involvement of a novel ADP-ribosylation factor GTPase-activating protein, SMAP, in membrane trafficking: implications in cancer cell biology.

P2860

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P2860

A new paxillin-binding protein, PAG3/Papalpha/KIAA0400, bearing an ADP-ribosylation factor GTPase-activating protein activity, is involved in paxillin recruitment to focal adhesions and cell migration

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http://www.wikidata.org/entity/Q24548827

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2000 nî lūn-bûn

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2000 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2000年の論文

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