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J. Biol. Chem., Vol. 275, Issue 31, 23615-23619, August 4, 2000
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From the Department of Biology, Technion-Israel Institute of
Technology, Haifa 32000, Israel
The binding of the coat protein complex,
coatomer, to the Golgi is mediated by the small GTPase
ADP-ribosylation factor-1 (ARF1), whereas the dissociation of coatomer,
requires GTP hydrolysis on ARF1, which depends on a GTPase-activating
protein (GAP). Recent studies demonstrate that when GAP activity is
assayed in a membrane-free environment by employing an amino-terminal
truncation mutant of ARF1 (
Role of Coatomer and Phospholipids in GTPase-activating
Protein-dependent Hydrolysis of GTP by ADP-ribosylation
Factor-1*
,,
17-ARF1) and a catalytic fragment of the
ARF GTPase-activating protein GAP1, GTP hydrolysis is strongly
stimulated by coatomer (Goldberg, J., (1999) Cell 96, 893-902). In this study, we investigated the role of coatomer in GTP
hydrolysis on ARF1 both in solution and in a phospholipid environment.
When GTP hydrolysis was assayed in solution using 17-ARF1, coatomer
stimulated hydrolysis in the presence of the full-length GAP1 as well
as with a Saccharomyces cerevisiae ARF GAP (Gcs1) but had
no effect on hydrolysis in the presence of the phosphoinositide
dependent GAP, ASAP1. Using wild-type myristoylated ARF1
loaded with GTP in the presence of phospholipid vesicles, GAP1 by
itself stimulated GTP hydrolysis efficiently, and coatomer had no
additional effect. Disruption of the phospholipid vesicles with
detergent resulted in reduced GAP1 activity that was stimulated by
coatomer, a pattern that resembled 17-ARF1 activity. Our
findings suggest that in the biological membrane, the proximity between
ARF1 and its GAP, which results from mutual binding to membrane
phospholipids, may be sufficient for stimulation of ARF1 GTPase activity.
*
This study was supported by Grant 208/97 from the
Israel Science Foundation.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.
These authors contributed equally to this work.
§
To whom correspondence should be addressed. Tel.:
972-4-829-3408; Fax: 972-4-822-5153; E-mail:
danc@techunix.technion.ac.il.
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