ArticleMolecular biology of the cell2001
An ADP-ribosylation factor GTPase-activating protein Git2-short/KIAA0148 is involved in subcellular localization of paxillin and actin cytoskeletal organization.
Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 89 citations in OpenAlex.
- The Arf family GTPases: Regulation of vesicle biogenesis and beyond.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Review
- Genetics of mirror movements identifies a multifunctional complex required for Netrin-1 guidance and lateralization of motor control.Science advances · 2023Article
- Article
- The Arf-GAP and protein scaffold Cat1/Git1 as a multifaceted regulator of cancer progression.Small GTPases · 2020Review
- Cool-associated Tyrosine-phosphorylated Protein 1 Is Required for the Anchorage-independent Growth of Cervical Carcinoma Cells by Binding Paxillin and Promoting AKT Activation.The Journal of biological chemistry · 2017Article
- Expanding functions of GIT Arf GTPase-activating proteins, PIX Rho guanine nucleotide exchange factors and GIT-PIX complexes.Journal of cell science · 2016Review
- Regulators and Effectors of Arf GTPases in Neutrophils.Journal of immunology research · 2015Review
- ARAP2 signals through Arf6 and Rac1 to control focal adhesion morphology.The Journal of biological chemistry · 2013Article
- The adaptor protein and Arf GTPase-activating protein Cat-1/Git-1 is required for cellular transformation.The Journal of biological chemistry · 2012Article
- GBF1 bears a novel phosphatidylinositol-phosphate binding module, BP3K, to link PI3Kγ activity with Arf1 activation involved in GPCR-mediated neutrophil chemotaxis and superoxide production.Molecular biology of the cell · 2012Article
- Cross talk between focal adhesion kinase and cadherins: role in regulating endothelial barrier function.Microvascular research · 2012Review
- Models for the functions of Arf GAPs.Seminars in cell & developmental biology · 2011Review
- Toward a model for Arf GTPases as regulators of traffic at the Golgi.FEBS letters · 2009Review
- Enhanced interaction between focal adhesion and adherens junction proteins: involvement in sphingosine 1-phosphate-induced endothelial barrier enhancement.Microvascular research · 2009Article
- EphA2 engages Git1 to suppress Arf6 activity modulating epithelial cell-cell contacts.Molecular biology of the cell · 2009Article
- The PIX-GIT complex: a G protein signaling cassette in control of cell shape.Seminars in cell & developmental biology · 2008Review
- AlphaPIX Rho GTPase guanine nucleotide exchange factor regulates lymphocyte functions and antigen receptor signaling.Molecular and cellular biology · 2008Article
- Fbx8 makes Arf6 refractory to function via ubiquitination.Molecular biology of the cell · 2008Article
- GIT1 utilizes a focal adhesion targeting-homology domain to bind paxillin.Cellular signalling · 2007Article
- GIT2 represses Crk- and Rac1-regulated cell spreading and Cdc42-mediated focal adhesion turnover.The EMBO journal · 2006Article
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Authors and funding
11 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Paxillin acts as an adaptor protein in integrin signaling. We have shown that paxillin exists in a relatively large cytoplasmic pool, including perinuclear areas, in addition to focal complexes formed at the cell periphery and focal adhesions formed underneath the cell. Several ADP-ribosylation factor (ARF) GTPase-activating proteins (GAPs; ARFGAPs) have been shown to associate with paxillin. We report here that Git2-short/KIAA0148 exhibits properties of a paxillin-associated ARFGAP and appears to be colocalized with paxillin, primarily at perinuclear areas. A fraction of Git2-short was also localized to actin-rich structures at the cell periphery. Unlike paxillin, however, Git2-short did not accumulate at focal adhesions underneath the cell. Git2-short is a short isoform of Git2, which is highly homologous to p95PKL, another paxillin-binding protein, and showed a weaker binding affinity toward paxillin than that of Git2. The ARFGAP activities of Git2 and Git2-short have been previously demonstrated in vitro, and we provided evidence that at least one ARF isoform, ARF1, is an intracellular substrate for the GAP activity of Git2-short. We also showed that Git2-short could antagonize several known ARF1-mediated phenotypes: overexpression of Git2-short, but not its GAP-inactive mutant, caused the redistribution of Golgi protein beta-COP and reduced the amounts of paxillin-containing focal adhesions and actin stress fibers. Perinuclear localization of paxillin, which was sensitive to ARF inactivation, was also affected by Git2-short overexpression. On the other hand, paxillin localization to focal complexes at the cell periphery was unaffected or even augmented by Git2-short overexpression. Therefore, an ARFGAP protein weakly interacting with paxillin, Git2-short, exhibits pleiotropic functions involving the regulation of Golgi organization, actin cytoskeletal organization, and subcellular localization of paxillin, all of which need to be coordinately regulated during integrin-mediated cell adhesion and intracellular signaling.
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