Article
- The EMBO Journal (2000) 19, 862 - 869
- doi:10.1093/emboj/19.5.862
TRAPP stably associates with the Golgi and is required for vesicle docking
Jemima Barrowman1,2, Michael Sacher1,2 and Susan Ferro-Novick1
- Howard Hughes Medical Institute and the Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06519, USA
- J.Barrowman and M.Sacher contributed equally to this work
Correspondence to:
Susan Ferro-Novick, E-mail: susan.ferronovick@yale.edu
Received 12 October 1999; Accepted 21 December 1999; Revised 21 December 1999
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.
Keywords:
- Bet3p,
- ER–Golgi transport,
- membrane traffic,
- TRAPP,
- vesicle docking
