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PMID: 10698928 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

TRAPP stably associates with the Golgi and is required for vesicle docking.

The EMBO journal ·Vol. 19 ·No. 5 ·2000-03-01 ·Pages 862-9

Barrowman J, Sacher M, Ferro-Novick S

Abstract

Bet3p, a component of a large novel complex called TRAPP, acts upstream of endoplasmic reticulum (ER)-Golgi SNAREs. Unlike the SNAREs, which reside on multiple compartments, Bet3p is localized exclusively to Golgi membranes. While other proteins recycle from the Golgi to the ER, Bet3p and other TRAPP subunits remain associated with this membrane under conditions that block anterograde traffic. We propose that the persistent localization of TRAPP to the Golgi may be important for its role in docking vesicles to this membrane. Consistent with this proposal, we find that transport vesicles fail to bind to Golgi membranes in vitro in the absence of Bet3p. Binding is restored by the addition of cytosol containing Bet3p. These findings indicate that TRAPP stably associates with the Golgi and is required for vesicle docking.

MeSH Terms
Animals Biological Transport Carrier Proteins/metabolism Cell Compartmentation Cell Line Cytoplasmic Granules/metabolism Endoplasmic Reticulum/metabolism Golgi Apparatus/metabolism Membrane Proteins/metabolism Vesicular Transport Proteins
Chemicals
Carrier Proteins Membrane Proteins Vesicular Transport Proteins transport protein particle, TRAPP
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Barrowman J
Howard Hughes Medical Institute, Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06519, USA.
Sacher M
Ferro-Novick S
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
DOI
10.1093/emboj/19.5.862
Published
2000-03-01
Pages
862-9
Language
English
Region
England
NLM ID
8208664
PMCID
PMC305626
Subset
IM
External Links
PubMed source DOI: 10.1093/emboj/19.5.862 PMC Full Text View journal details
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