A t-SNARE of the endocytic pathway must be activated for fusion Journal Article


Authors: Paumet, F.; Brügger, B.; Parlati, F.; Mcnew, J. A.; Söllner, T. H.; Rothman, J. E.
Article Title: A t-SNARE of the endocytic pathway must be activated for fusion
Abstract: The t-SNARE in a late Golgi compartment (Tlg2p) syntaxin is required for endocytosis and localization of cycling proteins to the late Golgi compartment in yeast. We show here that Tlg2p assembles with two light chains, Tlg1p and Vti1p, to form a functional t-SNARE that mediates fusion, specifically with the v-SNAREs Snc1p and Snc2p. In vitro, this t-SNARE is inert, locked in a nonfunctional state, unless it is activated for fusion. Activation can be mediated by a peptide derived from the v-SNARE, which likely bypasses additional regulatory proteins in the cell. Locking t-SNAREs creates the potential for spatial and temporal regulation of fusion by signaling processes that unleash their fusion capacity.
Keywords: nonhuman; protein localization; membrane proteins; amino acid sequence; molecular sequence data; saccharomyces cerevisiae; carrier proteins; protein transport; saccharomyces cerevisiae proteins; endocytosis; polyacrylamide gel electrophoresis; regulator protein; fusion; endosome; golgi complex; fungal proteins; vesicular transport proteins; membrane transport proteins; membrane fusion; snare protein; qa-snare proteins; qb-snare proteins; golgi apparatus; r-snare proteins; snare proteins; snare; priority journal; article; snc2p; tlg2p
Journal Title: Journal of Cell Biology
Volume: 155
Issue: 6
ISSN: 0021-9525
Publisher: Rockefeller University Press  
Date Published: 2001-12-10
Start Page: 961
End Page: 968
Language: English
DOI: 10.1083/jcb.200104092
PUBMED: 11739407
PROVIDER: scopus
PMCID: PMC2150898
DOI/URL:
Notes: Export Date: 21 May 2015 -- Source: Scopus
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MSK Authors
  1. Thomas H Sollner
    65 Sollner
  2. James E Rothman
    120 Rothman
  3. Fabienne Paumet
    7 Paumet
  4. Francesco Parlati
    17 Parlati