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Three novel proteins of the syntaxin/SNAP-25 family.


Intracellular membrane traffic is thought to be regulated in part by soluble N-ethylmaleimide-sensitive factor-attachment protein receptors (SNAREs) through the formation of complexes between these proteins present on vesicle and target membranes. All known SNARE-mediated fusion events involve members of the syntaxin and vesicle-associated membrane protein families. The diversity of mammalian membrane compartments predicts the existence of a large number of different syntaxin and vesicle-associated membrane protein genes. To further investigate the spectrum of SNAREs and their roles in membrane trafficking we characterized three novel members of the syntaxin and SNAP-25 (synaptosome-associated protein of 25 kDa) subfamilies. The proteins are broadly expressed, suggesting a general role in vesicle trafficking, and localize to distinct membrane compartments. Syntaxin 8 co-localizes with markers of the endoplasmic reticulum. Syntaxin 17, a divergent member of the syntaxin family, partially overlaps with endoplasmic reticulum markers, and SNAP-29 is broadly localized on multiple membranes. SNAP-29 does not contain a predicted membrane anchor characteristic of other SNAREs. In vitro studies established that SNAP-29 is capable of binding to a broad range of syntaxins.

Pubmed ID: 9852078


  • Steegmaier M
  • Yang B
  • Yoo JS
  • Huang B
  • Shen M
  • Yu S
  • Luo Y
  • Scheller RH


The Journal of biological chemistry

Publication Data

December 18, 1998

Associated Grants


Mesh Terms

  • Amino Acid Sequence
  • Animals
  • Blotting, Northern
  • COS Cells
  • Cell Line
  • Databases, Factual
  • Endoplasmic Reticulum
  • Ethylmaleimide
  • Evolution, Molecular
  • Humans
  • Membrane Proteins
  • Molecular Sequence Data
  • Multigene Family
  • Nerve Tissue Proteins
  • Phylogeny
  • Qa-SNARE Proteins
  • Rats
  • Recombinant Proteins
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Synaptosomal-Associated Protein 25
  • Transfection