Article
- The EMBO Journal (1998) 17, 2494 - 2503
- doi:10.1093/emboj/17.9.2494
TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion
Michael Sacher1, Yu Jiang2, Jemima Barrowman1, Al Scarpa1, Judy Burston1, Li Zhang1, David Schieltz3, John R. Yates III3, Hagai Abeliovich1 and Susan Ferro-Novick1
- Howard Hughes Medical Institute and the Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510, USA
- Present address: Department of Molecular Biology, Princeton University, Washington Road, Princeton, NJ 08544, USA
- Department of Molecular Biotechnology, University of Washington, Seattle, WA 98195-7730, USA
Correspondence to:
Susan Ferro-Novick, E-mail: susan_ferronovick@qm.yale.edu
Received 15 January 1998; Accepted 27 February 1998; Revised 27 February 1998
Abstract
We previously identified BET3 by its genetic interactions with BET1, a gene whose SNARE-like product acts in endoplasmic reticulum (ER)-to-Golgi transport. To gain insight into the function of Bet3p, we added three c-myc tags to its C-terminus and immunopurified this protein from a clarified detergent extract. Here we report that Bet3p is a member of a large complex (
800 kDa) that we call TRAPP (transport protein particle). We propose that TRAPP plays a key role in the targeting and/or fusion of ER-to-Golgi transport vesicles with their acceptor compartment. The localization of Bet3p to the cis-Golgi complex, as well as biochemical studies showing that Bet3p functions on this compartment, support this hypothesis. TRAPP contains at least nine other constituents, five of which have been identified and shown to be highly conserved novel proteins.
Keywords:
- membrane traffic,
- novel complex,
- vesicle targeting and fusion
