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

Michael Sacher, Yu Jiang, Jemima Barrowman, Al Scarpa, Judy Burston, Li Zhang, David Schieltz, John R. Yates, Hagai Abeliovich, Susan Ferro-Novick*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

243 Scopus citations

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.

Original languageAmerican English
Pages (from-to)2494-2503
Number of pages10
JournalEMBO Journal
Volume17
Issue number9
DOIs
StatePublished - 1 May 1998
Externally publishedYes

Keywords

  • Membrane traffic
  • Novel complex
  • Vesicle targeting and fusion

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