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

Proc Natl Acad Sci U S A. 2004 Mar 9;101(10):3376-80. doi: 10.1073/pnas.0400271101. Epub 2004 Feb 23.

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Motifs
  • Base Sequence
  • DNA, Fungal / genetics
  • Endocytosis
  • Membrane Fusion / genetics*
  • Membrane Fusion / physiology*
  • Membrane Proteins / chemistry
  • Membrane Proteins / genetics*
  • Membrane Proteins / metabolism*
  • Protein Structure, Tertiary
  • R-SNARE Proteins
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • SNARE Proteins
  • Saccharomyces cerevisiae / genetics*
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins / genetics*
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Vesicular Transport Proteins*

Substances

  • DNA, Fungal
  • Membrane Proteins
  • R-SNARE Proteins
  • Recombinant Fusion Proteins
  • SNARE Proteins
  • SNC2 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Vesicular Transport Proteins