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Titolo:
An ADP-ribosylation factor GTPase-activating protein Git2-short/KIAA0148 is involved in subcellular localization of paxillin and actin cytoskeletal organization
Autore:
Mazaki, Y; Hashimoto, S; Okawa, K; Tsubouchi, A; Nakamura, K; Yagi, R; Yano, H; Kondo, A; Iwamatsu, A; Mizoguchi, A; Sabe, H;
Indirizzi:
Osaka Biosci Inst, Dept Mol Biol, Osaka 5650874, Japan Osaka Biosci Inst Osaka Japan 5650874 ept Mol Biol, Osaka 5650874, Japan Kirin Brewery Co Ltd, Cent Labs Key Technol, Yokohama, Kanagawa 239, JapanKirin Brewery Co Ltd Yokohama Kanagawa Japan 239 ama, Kanagawa 239, Japan Kyoto Univ, Grad Sch Biostudies, Sakyo Ku, Kyoto 6068502, Japan Kyoto Univ Kyoto Japan 6068502 iostudies, Sakyo Ku, Kyoto 6068502, Japan Japan Sci & Technol Corp, Kyoto 6190237, Japan Japan Sci & Technol Corp Kyoto Japan 6190237 Corp, Kyoto 6190237, Japan
Titolo Testata:
MOLECULAR BIOLOGY OF THE CELL
fascicolo: 3, volume: 12, anno: 2001,
pagine: 645 - 662
SICI:
1059-1524(200103)12:3<645:AAFGPG>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
ZINC-FINGER MOTIF; BINDING-PROTEIN; TYROSINE PHOSPHORYLATION; GOLGI MEMBRANES; ENDOPLASMIC-RETICULUM; FOCAL ADHESIONS; PHOSPHOLIPASE-D; CELL-MIGRATION; POTENTIAL ROLE; CHOLERA-TOXIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
79
Recensione:
Indirizzi per estratti:
Indirizzo: Sabe, H Osaka Biosci Inst, Dept Mol Biol, Osaka 5650874, Japan Osaka Biosci Inst Osaka Japan 5650874 Biol, Osaka 5650874, Japan
Citazione:
Y. Mazaki et al., "An ADP-ribosylation factor GTPase-activating protein Git2-short/KIAA0148 is involved in subcellular localization of paxillin and actin cytoskeletal organization", MOL BIOL CE, 12(3), 2001, pp. 645-662

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 evidencethat at least one ARF isoform, ARF1, is an intracellular substrate for theGAP? activity of Git2-short. We also showed that Git2-short could antagonize several known ARF1-mediated phenotypes: overexpression of Git2-short, but not its GAF-inactive mutant, caused the redistribution of Golgi protein beta -COP and reduced the amounts of paxillin-containing focal adhesions andactin 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 01:53:23