Syntaxins are the prototype family of SNARE [soluble NSF (N-ethylmaleimide-sensitive fusion protein)-attachment protein receptor] proteins involved in the membrane fusion process of synaptic vesicles with the presynaptic plasma membrane. In the exocytic and the endocytic pathway, syntaxins can mediate vesicle fusion in diverse vesicular transport processes through binding to other SNAREs and with the cytoplasmic NSF and SNAP. Besides, syntaxins can bind synaptotagmin in a calcium-dependent fashion and interact with voltage-dependent calcium and potassium channels involved in the depolarization of the presynaptic axonal boutons. Syntaxins have a similar structure that contains a single C-terminal pass-membrane domain, a SNARE domain, and an N-terminal domain. The SNARE domain can bind to both synaptobrevin and SNAP-25 forming the core SNARE complex which provides the free energy for initiating the fusion of vesicle membrane and plasma membrane. The N-terminal domain is a regulator of syntaxin conformation.
There are 15 members of the syntaxin family in the human genome. Here shows part of syntaxins in humans including STX1A, STX7, and STX8. STX1A plays an essential role in the regulation of ion channel and synaptic exocytosis. STX8 can form the SNARE complex with syntaxin 7, vti1b and endobrevin participating in the homotypic fusion of late endosomes.
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