The ARF1 GTPase-activating protein: zinc finger motif and Golgi complex localization.
Science
; 270(5244): 1999-2002, 1995 Dec 22.
Article
en En
| MEDLINE
| ID: mdl-8533093
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.
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Bases de datos:
MEDLINE
Asunto principal:
Proteínas
/
Dedos de Zinc
/
Proteínas de Unión al GTP
/
Aparato de Golgi
Tipo de estudio:
Prognostic_studies
Límite:
Animals
Idioma:
En
Revista:
Science
Año:
1995
Tipo del documento:
Article
País de afiliación:
Israel