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首页> 外文OA文献 >An ADP-Ribosylation Factor GTPase-activating Protein Git2-short/KIAA0148 Is Involved in Subcellular Localization of Paxillin and Actin Cytoskeletal Organization
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An ADP-Ribosylation Factor GTPase-activating Protein Git2-short/KIAA0148 Is Involved in Subcellular Localization of Paxillin and Actin Cytoskeletal Organization

机译：ADP-核糖基化因子GTP酶激活蛋白 Git2-short / KIAA0148参与Paxillin的亚细胞定位 和肌动蛋白细胞骨架组织

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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 β-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.
机译：Paxillin在整合素信号传导中充当衔接蛋白。我们已经表明，除了在细胞外围形成的局灶复合物和在细胞下方形成的局灶性粘连之外，帕西林还存在于相对较大的细胞质库中，包括核周区域。几种ADP-核糖基化因子（ARF）GTP酶激活蛋白（GAP; ARFGAP）已显示与Paxillin相关。我们在这里报告，Git2-short / KIAA0148表现出与paxillin相关的ARFGAP的属性，并且似乎与paxillin共定位，主要在核周区域。 Git2-short的一部分也位于细胞外围富含肌动蛋白的结构。但是，与paxillin不同，Git2-short不会积聚在细胞下方的粘连处。 Git2-short是Git2的短同种型，与另一种paxillin结合蛋白p95PKL高度同源，并且对paxillin的结合亲和力比Git2弱。 Git2和Git2-short的ARFGAP活性先前已在体外得到证实，我们提供的证据表明，至少一种ARF亚型ARF1是Git2-short的GAP活性的细胞内底物。我们还表明，Git2-short可以拮抗几种已知的ARF1介导的表型：Git2-short的过表达，但不是GAP失活的突变体，导致高尔基体蛋白β-COP的重新分布，并减少了含Paxillin的粘着斑和肌动蛋白应力纤维。对ARF失活敏感的paxillin的核周定位也受到Git2短时过表达的影响。另一方面，Git2-short的过表达不会影响甚至使paxillin定位于细胞周围的局灶复合物。因此，ARFGAP蛋白与Paxillin弱相互作用，即Git2-short，表现出多效性功能，涉及高尔基体组织，肌动蛋白细胞骨架组织和Paxillin的亚细胞定位的调节，所有这些都需要在整合素介导的细胞粘附和细胞内过程中进行协调调节。信号。

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