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- W2019031014 abstract "The ADP-ribosylation factor (ARF) 6 small GTPase regulates vesicle trafficking and cytoskeletal actin reorganization. The GTPase-activating proteins (GAPs) catalyze the formation of inactive ARF6GDP. Centaurin-α1 contains an ARF GAP and two pleckstrin homology (PH) domains, which bind the second messenger phosphatidylinositol 3,4,5-trisphosphate (PIP3). Here, we show that centaurin-α1 specifically inhibits in vivo GTP loading of ARF6 and redistribution of ARF6 from the endosomal compartment to the plasma membrane, which are indicative of its activation. Centaurin-α1 also inhibited cortical actin formation in a PIP3-dependent manner. Moreover, the constitutively active mutant of ARF6, but not that of ARF1, reverses the inhibition of cortical actin formation by centaurin-α1. An artificially plasma membrane-targeted centaurin-α1 bypasses the requirement of PIP3 for its involvement in ARF6 inactivation, suggesting that PIP3 is required for recruitment of centaurin-α1 to the plasma membrane but not for its activity. Together, these data suggest that centaurin-α1 negatively regulates ARF6 activity by functioning as an in vivo PIP3-dependent ARF6 GAP." @default.
- W2019031014 created "2016-06-24" @default.
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- W2019031014 date "2004-02-01" @default.
- W2019031014 modified "2023-10-10" @default.
- W2019031014 title "Centaurin-α1 Is an in Vivo Phosphatidylinositol 3,4,5-Trisphosphate-dependent GTPase-activating Protein for ARF6 That Is Involved in Actin Cytoskeleton Organization" @default.
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- W2019031014 doi "https://doi.org/10.1074/jbc.c300482200" @default.
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