Complexin-1 (CPLX1)

Complexin-1 is a small, highly charged cytosolic protein encoded by the CPLX1 gene, primarily expressed in the nervous system[1][2][4]. It binds to the neuronal SNARE complex (comprising synaptobrevin, syntaxin, and SNAP-25), acting as a central regulator of synaptic vesicle exocytosis and neurotransmitter release[1][3][4][7]. Complexin-1 has several domains with distinct roles: the N-terminal domain activates synchronous, calcium-triggered transmitter release; the accessory domain regulates spontaneous release; the central domain is required for all functions; and the C-terminal domain is involved in vesicle priming and membrane binding[3][5]. Complexin-1 is crucial for the precise timing and regulation of neurotransmitter release, functioning both to activate evoked (stimulus-dependent) release and to regulate spontaneous release events, possibly acting as a checkpoint during synaptic vesicle fusion machinery assembly[3][5][7]. Genetic mutations in CPLX1 are implicated in severe neurodevelopmental disorders, including early infantile epileptic encephalopathy (EIEE63/DEE63)[1]. CPLX1 interacts with proteins such as SNAP-25 and syntaxin-1A[1]. It is not a direct therapeutic target itself (i.e., not a receptor, enzyme, or transporter commonly targeted by drugs), and no drugs currently target Complexin-1 or use it as a biomarker.

Other names

Complexin-1CPLX1CPX ICPX-IComplexin ISynaphin-2DEE63EIEE63complexin-1complexin Isynaphin 2