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SNARE (protein)
SNARE proteins (an acronym derived from "SNAP (Soluble NSF Attachment Protein) REceptor") are a large protein superfamily consisting of more than 60 members in yeast and mammalian cells.〔
〕 The primary role of SNARE proteins is to mediate vesicle fusion, that is, the fusion of vesicles with their target membrane bound compartments (such as a lysosome). The best studied SNAREs are those that mediate docking of synaptic vesicles with the presynaptic membrane in neurons. These SNAREs are the targets of the bacterial neurotoxins responsible for botulism and tetanus.
== Types ==
SNAREs can be divided into two categories: ''vesicle'' or ''v-SNAREs'', which are incorporated into the membranes of transport vesicles during budding, and ''target'' or ''t-SNAREs'', which are located in the membranes of target compartments. Evidence suggests that t-SNAREs form stable subcomplexes which serve as guides for v-SNARE binding to complete the formation of the SNARE complex. Several SNARE proteins are located on both vesicles and target membranes, therefore, a more recent classification scheme takes into account structural features of SNAREs, dividing them into R-SNAREs and Q-SNAREs. Often, R-SNAREs act as v-SNAREs and Q-SNAREs act as t-SNAREs. R-SNAREs are proteins that contribute an arginine (R) residue in the formation of the zero ionic layer in the assembled core SNARE complex. One particular R-SNARE is synaptobrevin, which is located in the synaptic vesicles. Q-SNAREs are proteins that contribute a glutamine (Q) residue in the formation of the zero ionic layer in the assembled core SNARE complex. Q-SNAREs include syntaxin and SNAP-25. Q-SNAREs are further classified as Qa, Qb, or Qc depending on their location in the four-helix bundle.
抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』
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