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Vol. 12, Issue 3, 645-662, March 2001
¶
*Department of Molecular Biology, Osaka Bioscience Institute,
Suita, Osaka 565-0874, Japan; 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 Central Laboratories for
Key Technology, Kirin Brewery Company Ltd., Yokohama, Kanagawa 239, Japan; §Graduate School of Medicine and
Graduate School of Biostudies, Kyoto University,
Sakyoku, Kyoto 606-8502, Japan; and Precursory Research
for Embryonic Science and Technology, Japan Science and Technology
Corporation, Kyoto 619-0237, Japan
-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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