TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion.

M Sacher, Y Jiang, J Barrowman, A Scarpa, J Burston, L Zhang, D Schieltz, J R Yates, H Abeliovich, S Ferro-Novick

Howard Hughes Medical Institute and the Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06510, USA.

The EMBO journal 1998 May 1

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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 ( approximately 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.

Citation

M Sacher, Y Jiang, J Barrowman, A Scarpa, J Burston, L Zhang, D Schieltz, J R Yates, H Abeliovich, S Ferro-Novick. TRAPP, a highly conserved novel complex on the cis-Golgi that mediates vesicle docking and fusion. The EMBO journal. 1998 May 1;17(9):2494-503