SNARE protein

Molecular machinery driving vesicle fusion in neuromediator release. The core SNARE complex is formed by four α-helices contributed by synaptobrevin, syntaxin and SNAP-25, synaptotagmin serves as a calcium sensor and closely regulates the SNARE zipping.[1]
SNARE-fusion membrane complex proteins
Identifiers
SymbolSNARE
InterProIPR010989
SCOP21kil / SCOPe / SUPFAM
TCDB1.F.1
OPM superfamily197
OPM protein3hd7
Membranome198

SNARE proteins – "SNAP REceptors" – are a large protein family consisting of at least 24 members in yeasts and more than 60 members in mammalian and plant cells.[2][3][4] The primary role of SNARE proteins is to mediate the fusion of vesicles with the target membrane; this notably mediates exocytosis, but can also mediate the fusion of vesicles with membrane-bound compartments (such as a lysosome). The best studied SNAREs are those that mediate the release of synaptic vesicles containing neurotransmitters in neurons. These neuronal SNAREs are the targets of the neurotoxins responsible for botulism and tetanus produced by certain bacteria.

  1. ^ Georgiev DD, Glazebrook JF (2007). "Subneuronal processing of information by solitary waves and stochastic processes". In Lyshevski SE (ed.). Nano and Molecular Electronics Handbook (PDF). Nano and Microengineering Series. CRC Press. pp. 17–1–17–41. doi:10.1201/9781315221670. ISBN 978-0-8493-8528-5.
  2. ^ Burri L, Lithgow T (January 2004). "A complete set of SNAREs in yeast". Traffic. 5 (1): 45–52. doi:10.1046/j.1600-0854.2003.00151.x. PMID 14675424. S2CID 45480417.
  3. ^ Gerald K (2002). Cell and Molecular Biology (4th ed.). John Wiley & Sons.
  4. ^ Gu X, Brennan A, Wei W, Guo G, Lindsey K (October 2020). "Vesicle Transport in Plants: A Revised Phylogeny of SNARE Proteins". Evolutionary Bioinformatics. 16. doi:10.1177/1176934320956575.