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J Biol Chem, Vol. 275, Issue 18, 13901-13906, May 5, 2000
From ADP-ribosylation factor (ARF) proteins are key
players in numerous vesicular trafficking events ranging from the
formation and fusion of vesicles in the Golgi apparatus to exocytosis
and endocytosis. To complete their GTPase cycle, ARFs require a guanine nucleotide-exchange protein to catalyze replacement of GDP by GTP and a
GTPase-activating protein (GAP) to accelerate hydrolysis of bound GTP.
Recently numerous guanine nucleotide-exchange proteins and GAP proteins
have been identified and partially characterized. Every ARF GAP protein
identified to date contains a characteristic zinc finger motif. GIT1
and GIT2, two members of a new family of G protein-coupled receptor
kinase-interacting proteins, also contain a putative zinc finger motif
and display ARF GAP activity. Truncation of the amino-terminal region
containing the zinc finger motif prevented GAP activity of GIT1. One
zinc molecule was found associated per molecule of purified recombinant
ARF-GAP1, GIT1, and GIT2 proteins, suggesting the zinc finger motifs of
ARF GAPs are functional and should play an important role in their GAP activity. Unlike ARF-GAP1, GIT1 and GIT2 stimulate hydrolysis of GTP
bound to ARF6. Accordingly we found that the phospholipid dependence of
the GAP activity of ARF-GAP1 and GIT proteins was quite different, as
the GIT proteins are stimulated by phosphatidylinositol 3,4,5-trisphosphate whereas ARF-GAP1 is stimulated by
phosphatidylinositol 4,5-bisphosphate and diacylglycerol. These results
suggest that although the mechanism of GTP hydrolysis is probably very
similar in these two families of ARF GAPs, GIT proteins might
specifically regulate the activity of ARF6 in cells in coordination
with phosphatidylinositol 3-kinase signaling pathways.
GIT Proteins, A Novel Family of Phosphatidylinositol
3,4,5-Trisphosphate-stimulated GTPase-activating Proteins for ARF6*
§,
,, and INSERM U-338, Centre de Neurochimie, 5 rue
Blaise Pascal, 67084 Strasbourg Cedex, France, the
** Departments of Medicine (Cardiology and
Gastroenterology) and Biochemistry, Howard Hughes Medical
Institute, Duke University Medical Center, Durham, North Carolina
27710, and the ¶ Pulmonary-Critical Care Medicine
Branch, NHLBI, National Institutes of Health,
Bethesda, Maryland 20892
*
This work was supported in part by National Institutes of
Health Grant HL16037 (to R. J. L.).The costs of publication of this article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Present address Dept. of Chemistry, Lebanon Valley College,
Annville, PA 17003.
Investigator of the Howard Hughes Medical Institute.
§§
To whom correspondence and reprint requests should be addressed:
Dept. of Medicine (Gastroenterology), Box 3083, Duke University Medical
Center, Durham, NC 27710. Tel.: 919-684-5620; Fax: 919-684-4983; E-mail: richard.premont@duke.edu.
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