Abstract
Hydrolysis of guanosine triphosphate (GTP) by the small guanosine triphosphatase (GTPase) adenosine diphosphate ribosylation factor-1 (ARF1) depends on a GTPase-activating protein (GAP). A complementary DNA encoding the ARF1 GAP was cloned from rat liver and predicts a protein with a zinc finger motif near the amino terminus. The GAP function required an intact zinc finger and additional amino-terminal residues. The ARF1 GAP was localized to the Golgi complex and was redistributed into a cytosolic pattern when cells were treated with brefeldin A, a drug that prevents ARF1-dependent association of coat proteins with the Golgi. Thus, the GAP is likely to be recruited to the Golgi by an ARF1-dependent mechanism.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
ADP-Ribosylation Factor 1
-
ADP-Ribosylation Factors
-
Alternative Splicing
-
Amino Acid Sequence
-
Animals
-
Base Sequence
-
Brefeldin A
-
Cloning, Molecular
-
Cyclopentanes / pharmacology
-
Cytosol / metabolism
-
DNA, Complementary
-
GTP-Binding Proteins / metabolism*
-
GTPase-Activating Proteins
-
Golgi Apparatus / metabolism*
-
Guanosine Triphosphate / metabolism
-
Liver / metabolism
-
Molecular Sequence Data
-
Proteins / chemistry
-
Proteins / genetics
-
Proteins / isolation & purification
-
Proteins / metabolism*
-
Rats
-
Zinc Fingers*
Substances
-
Cyclopentanes
-
DNA, Complementary
-
GTPase-Activating Proteins
-
Proteins
-
Brefeldin A
-
Guanosine Triphosphate
-
GTP-Binding Proteins
-
ADP-Ribosylation Factor 1
-
ADP-Ribosylation Factors