Syntax ins are a family of membrane integrated Q-SNARE proteins participating in exocytosis (1). They possess a single C-terminal transmembrane domain, a SNARE domain, and an N-terminal regulatory domain. This SNARE domain binds to synaptobrevin and SNAP-25 to form the SNARE complex (2, 3).
Support of syntaxin’s involvement in vesicular transport and neurotransmission includes the requirement of its yeast homologs, SSO 1 and 2, in targeting and fusion of Golgi-derived vesicles with the plasma membrane (4). Syntaxin also provides the target pf clostridial neurotoxin C1, which blocks neurotransmitter release (5). The formation of 20S complex involves the interaction of VAMP with syntaxin through an ATP-dependent reaction modulated by synaptotagmin, SNAP-25, a-SNAP and NSF (6).