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Complexins: cytosolic proteins that regulate SNAP receptor function.

A family of proteins called complexins was discovered that compete with alpha-SNAP, but not synaptotagmin, for SNAP receptor binding. Complexins I and II are highly homologous hydrophilic proteins that are tightly conserved, with 100% identity among mouse, rat, and human complexin II. They are enriched in neurons where they colocalize with syntaxin and SNAP-25; in addition, complexin II is expressed ubiquitously at low levels. Complexins bind weakly to syntaxin alone and not at all to synaptobrevin and SNAP-25, but strongly to the SNAP receptor-core complex composed of these three molecules. They compete with alpha-SNAP for binding to the core complex but not with other interacting molecules, including synaptotagmin I, suggesting that the complexins regulate the sequential interactions of alpha-SNAP and synaptotagmins with the SNAP receptor during exocytosis.

Pubmed ID: 7553862

Authors

  • McMahon HT
  • Missler M
  • Li C
  • S├╝dhof TC

Journal

Cell

Publication Data

October 6, 1995

Associated Grants

None

Mesh Terms

  • Adaptor Proteins, Vesicular Transport
  • Amino Acid Sequence
  • Animals
  • Brain Chemistry
  • Calcium
  • Calcium-Binding Proteins
  • Carrier Proteins
  • Cytosol
  • Exocytosis
  • Gene Expression
  • Hippocampus
  • Humans
  • Macromolecular Substances
  • Membrane Fusion
  • Membrane Glycoproteins
  • Membrane Proteins
  • Mice
  • Molecular Sequence Data
  • Nerve Tissue Proteins
  • Neurons
  • R-SNARE Proteins
  • Rats
  • Recombinant Fusion Proteins
  • SNARE Proteins
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
  • Species Specificity
  • Synaptic Vesicles
  • Synaptosomal-Associated Protein 25
  • Synaptotagmin I
  • Synaptotagmins
  • Vesicular Transport Proteins