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Vol. 13, Issue 6, 2147-2156, June 2002
Department of Microbiology, University of Virginia Health System,
Charlottesville, Virginia 22908
ASAP1 (ADP ribosylation factor [ARF]- GTPase-activating protein
[GAP] containing SH3, ANK repeats, and PH domain) is a
phospholipid-dependent ARF-GAP that binds to and is phosphorylated by
pp60Src. Using affinity chromatography and yeast two-hybrid
interaction screens, we identified ASAP1 as a major binding partner of
protein tyrosine kinase focal adhesion kinase (FAK). Glutathione
S-transferase pull-down and coimmunoprecipitation assays
showed the binding of ASAP1 to FAK is mediated by an interaction
between the C-terminal SH3 domain of ASAP1 with the second proline-rich
motif in the C-terminal region of FAK. Transient overexpression of
wild-type ASAP1 significantly retarded the spreading of REF52 cells
plated on fibronectin. In contrast, overexpression of a truncated
variant of ASAP1 that failed to bind FAK or a catalytically inactive
variant of ASAP1 lacking GAP activity resulted in a less pronounced
inhibition of cell spreading. Transient overexpression of wild-type
ASAP1 prevented the efficient organization of paxillin and FAK in focal adhesions during cell spreading, while failing to significantly alter
vinculin localization and organization. We conclude from these studies
that modulation of ARF activity by ASAP1 is important for the
regulation of focal adhesion assembly and/or organization by
influencing the mechanisms responsible for the recruitment and
organization of selected focal adhesion proteins such as paxillin and
FAK.
Present address: GameSpy Industries, 18002 Skypark
Circle, Irvine, CA 92614
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