Synaptotagmin-5 (SYT5)

Synaptotagmin-5 (SYT5) is a member of the synaptotagmin family of type III membrane proteins, characterized by the presence of cytoplasmic C2 domains that are involved in calcium binding[2][3][6]. SYT5 localizes to membranes and plays a critical role in Ca2+-dependent exocytosis of secretory vesicles, likely acting as a calcium sensor during vesicular trafficking and exocytosis[2][3][6]. It is implicated in the regulation of neurotransmitter release, notably by modulating norepinephrine secretion and mediating export from endocytic recycling compartments to the cell surface[2]. Structurally, it shares the typical synaptotagmin architecture: an N-terminal transmembrane region, a synaptotagmin-like mitochondrial-lipid binding protein (SMP) domain, and two C2 domains, which confer its Ca2+-sensing and phospholipid-interacting capabilities[1]. SYT5 forms complexes with other synaptotagmins and likely contributes to the specificity of membrane tethering and vesicle fusion events[1]. While genetic or direct therapeutic targeting of SYT5 is not routinely described, it is classified as a putative molecular target given its defined biochemical function in exocytosis[2]. Disease associations in the literature include rare vascular events, but clear links to common conditions or established roles as a drug target are lacking[2][5].

Other names

Synaptotagmin-5SYT5SytVSynaptotagmin Vsynaptotagmin-5synaptotagmin VsytV