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Functional architecture of an intracellular membrane t-SNARE.

Lipid bilayer fusion is mediated by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) located on the vesicle membrane (v-SNAREs) and the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE complex consists of a bundle of four helices, of which one is supplied by the v-SNARE and the other three by the t-SNARE. For t-SNAREs on the plasma membrane, the protein syntaxin supplies one helix and a SNAP-25 protein contributes the other two. Although there are numerous homologues of syntaxin on intracellular membranes, there are only two SNAP-25-related proteins in yeast, Sec9 and Spo20, both of which are localized to the plasma membrane and function in secretion and sporulation, respectively. What replaces SNAP-25 in t-SNAREs of intracellular membranes? Here we show that an intracellular t-SNARE is built from a 'heavy chain' homologous to syntaxin and two separate non-syntaxin 'light chains'. SNAP-25 may thus be the exception rather than the rule, having been derived from genes that encoded separate light chains that fused during evolution to produce a single gene encoding one protein with two helices.

Pubmed ID: 11001059

Authors

  • Fukuda R
  • McNew JA
  • Weber T
  • Parlati F
  • Engel T
  • Nickel W
  • Rothman JE
  • Söllner TH

Journal

Nature

Publication Data

September 14, 2000

Associated Grants

None

Mesh Terms

  • Escherichia coli
  • Fungal Proteins
  • Intracellular Membranes
  • Membrane Proteins
  • Nerve Tissue Proteins
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Quaternary
  • Qa-SNARE Proteins
  • R-SNARE Proteins
  • Recombinant Fusion Proteins
  • SNARE Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Synaptosomal-Associated Protein 25
  • Vesicular Transport Proteins