Anti-phospho-Alpha-Synuclein (Tyr133)

SncA is a member of the synuclein family of structurally related proteins that are prominently expressed in the central nervous system, which also includes beta- and gamma-synuclein. Synucleins are abundantly expressed in the brain and SncA and Snc-Beta inhibit phospholipase D2 selectively. SncA may serve to integrate presynaptic signaling and membrane trafficking. Aggregated SncA proteins form brain lesions that are hallmarks of neurodegenerative synucleinopathies. Defects in SncA play a role in the pathogenesis of Parkinson disease. SncA peptides are a major component of amyloid plaques in the brains of patients with Alzheimer disease. SncA shares 95% sequence homology with rat SncA. Rat SncA is specifically expressed in brain and is associated with synaptosomal membranes in neurons Protein function: Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (PubMed:28288128, PubMed:30404828, PubMed:20798282, PubMed:26442590). Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores (PubMed:28288128, PubMed:30404828). Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis (PubMed:30404828). Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5 (PubMed:20798282). This chaperone activity is important to sustain normal SNARE-complex assembly during aging (PubMed:20798282). Plays also a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (PubMed:26442590). [The UniProt Consortium]