Syntaxin-1A (STX1A)

Syntaxin-1A is a membrane-anchored SNARE protein critical for synaptic vesicle exocytosis in neurons. It is predominantly found at the presynaptic active zone and facilitates the assembly of the core SNARE complex (with SNAP-25 and synaptobrevin/VAMP2), which drives fusion of neurotransmitter-containing vesicles with the plasma membrane. Syntaxin-1A cycles between ‘closed’ (inactive) and ‘open’ (fusion-competent) conformations, regulated by interacting proteins (e.g., Munc18-1). Its function is essential for rapid synaptic transmission, and its dysregulation is linked to neurological disorders. Toxins such as botulinum and tetanus block neurotransmitter release by proteolytically cleaving Syntaxin-1A or other SNARE proteins, illustrating its pivotal role in neuronal communication[1][2][3][5][8].

Other names

Syntaxin 1STX1At-SNARESyntaxin-1At-SNARE1A

Inhibitors such as botulinum neurotoxin and tetanus toxin cleave SNARE proteins (including Syntaxin-1A), blocking SNARE complex assembly and inhibiting neurotransmitter release[5]