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GDI1 ENCODES A GDP DISSOCIATION INHIBITOR THAT PLAYS AN ESSENTIAL ROLE IN THE YEAST SECRETORY PATHWAY
Author(s): GARRETT MD, ZAHNER JE, CHENEY CM, NOVICK PJ
Source: EMBO JOURNAL    Volume: 13    Issue: 7    Pages: 1718-1728    Published: APR 1 1994  
Times Cited: 131     References: 75     
Abstract: GTP binding proteins of the Sec4/Ypt/rab family regulate distinct vesicular traffic events in eukaryotic cells. We have cloned GD11, an essential homolog of bovine rab GDI (GDP dissociation inhibitor) from the yeast Saccharomyces cervisiae. Analogous to the bovine protein, purified Gdi1p slows the dissociation of GDP from Sec4p and releases the GDP-bound form from yeast membranes. Depletion of Gdi1p in vivo leads to loss of the soluble pool of Sec4p and inhibition of protein transport at multiple stages of the secretory pathway. Complementation analysis indicates that GD11 is allelic to sec19-1. These results establish that Gdi1p plays an essential function in membrane traffic and are consistent with a role for Gdi1p in the recycling of proteins of the Sec3/Ypt/rab family from their target membranes back to their vesicular pools.
Document Type: Article
Language: English
Addresses:
1. YALE UNIV, SCH MED, DEPT CELL BIOL, NEW HAVEN, CT 06510 USA
2. WASHINGTON UNIV, SCH MED, DEPT GENET, ST LOUIS, MO 63110 USA
Publisher: OXFORD UNIV PRESS UNITED KINGDOM, WALTON ST JOURNALS DEPT, OXFORD, ENGLAND OX2 6DP
Subject Category: Biochemistry & Molecular Biology; Cell Biology
IDS Number: NF928
ISSN: 0261-4189
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