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PMID: 1907973 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Sec12p-dependent membrane binding of the small GTP-binding protein Sar1p promotes formation of transport vesicles from the ER.

The Journal of cell biology ·Vol. 114 ·No. 4 ·1991-08-00 ·Pages 663-70

d'Enfert C, Wuestehube LJ, Lila T, Schekman R

Abstract

Sec12p is an integral membrane protein required in vivo and in vitro for the formation of transport vesicles generated from the ER. Vesicle budding and protein transport from ER membranes containing normal levels of Sec12p is inhibited in vitro by addition of microsomes isolated from a Sec12p-overproducing strain. Inhibition is attributable to titration of a limiting cytosolic protein. This limitation is overcome by addition of a highly enriched fraction of soluble Sar1p, a small GTP-binding protein, shown previously to be essential for protein transport from the ER and whose gene has been shown to interact genetically with sec12. Furthermore, Sar1p binding to isolated membranes is enhanced at elevated levels of Sec12p. Sar1p-Sec12p interaction may regulate the initiation of vesicle budding from the ER.

MeSH Terms
Cytosol/metabolism Endoplasmic Reticulum/metabolism GTP-Binding Proteins/metabolism Golgi Apparatus Kinetics Membrane Proteins/metabolism Microsomes/metabolism Models, Biological Plasmids Saccharomyces cerevisiae/genetics,metabolism
Chemicals
Membrane Proteins GTP-Binding Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
d'Enfert C
Division of Biochemistry and Molecular Biology, University of California, Berkeley 94720.
Wuestehube L J
Lila T
Schekman R
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
Published
1991-08-00
Pages
663-70
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2289894
Subset
IM
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