Synaptic vesicle glycoprotein 2 (SV2) (SV2)

Synaptic vesicle glycoprotein 2 (SV2) is a family of integral membrane proteins, comprising three isoforms (SV2A, SV2B, and SV2C), primarily located on the membranes of synaptic vesicles in neurons [1]. SV2A is ubiquitously expressed throughout the central nervous system, while SV2C is more selectively expressed in specific regions such as the striatum and cholinergic brainstem nuclei [2]. These proteins are essential for proper neurotransmitter release, acting as regulators of vesicle priming and calcium-dependent exocytosis [3]. SV2 isoforms are clinically significant as the high-affinity receptors for Botulinum neurotoxin type A (BoNT/A), which exploits the luminal domain of SV2 during vesicle recycling to enter cholinergic presynaptic terminals and inhibit acetylcholine release [4]. Furthermore, SV2A is the primary molecular target for the antiepileptic drugs levetiracetam and brivaracetam, which bind to the protein to modulate synaptic transmission and reduce seizure activity [5]. Recent advancements have also utilized SV2A as a PET imaging biomarker to quantify synaptic density in neurodegenerative conditions like Alzheimer's disease [6].

Other names

SV2ASV2BSV2CSynaptic vesicle protein 2Synaptic vesicle glycoprotein 2ASynaptic vesicle glycoprotein 2BSynaptic vesicle glycoprotein 2C

SV2 proteins regulate the probability of neurotransmitter release by modulating synaptic vesicle priming and calcium sensitivity [3]. They also act as receptors for Botulinum neurotoxins, which bind to the luminal domain of SV2 during vesicle recycling to undergo endocytosis into the presynaptic terminal [4].