The specificity of SNARE-dependent fusion is encoded in the SNARE motif Journal Article


Authors: Paumet, F.; Rahimian, V.; Rothman, J. E.
Article Title: The specificity of SNARE-dependent fusion is encoded in the SNARE motif
Abstract: Soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins constitute the core of the fusion machinery, and isolated SNAREs fuse membranes with exquisite specificity by cognate pairing. Most SNAREs have a membrane-spanning region, an N-terminal domain, and a membrane proximal SNARE motif domain. Although the SNARE motif is critical for SNARE complex formation, is it the sole determinant of the specificity of SNARE-dependent fusion? To test this, we make use of a SNARE complex functioning in the late endosomal compartment in yeast. Studying this complex and the previously identified early endosomal SNARE complex, we find that the specificity of fusion resides in the SNARE motifs.
Keywords: nonhuman; protein domain; protein motif; complex formation; membrane proteins; amino terminal sequence; recombinant fusion proteins; saccharomyces cerevisiae; membrane protein; base sequence; protein structure, tertiary; yeast; saccharomyces cerevisiae proteins; endocytosis; liposome; amino acid motifs; endosome; dna, fungal; vesicular transport proteins; membrane fusion; snare protein; saccharomyces; r-snare proteins; snare proteins; priority journal; article
Journal Title: Proceedings of the National Academy of Sciences of the United States of America
Volume: 101
Issue: 10
ISSN: 0027-8424
Publisher: National Academy of Sciences  
Date Published: 2004-03-09
Start Page: 3376
End Page: 3380
Language: English
DOI: 10.1073/pnas.0400271101
PROVIDER: scopus
PMCID: PMC373469
PUBMED: 14981247
DOI/URL:
Notes: Proc. Natl. Acad. Sci. U. S. A. -- Cited By (since 1996):47 -- Export Date: 16 June 2014 -- CODEN: PNASA -- Source: Scopus
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MSK Authors
  1. James E Rothman
    120 Rothman
  2. Fabienne Paumet
    7 Paumet
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