Recombinant human Alpha-synuclein (mutated A53T) protein monomer Type 1 (Active)

Specifications

Form

Liquid

Additional notes

Purified by ion-exchange chromatography.

General info

Function

Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release (PubMed : 20798282, PubMed : 26442590, PubMed : 28288128, PubMed : 30404828). 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). Also acts 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). Also plays a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity (PubMed : 26442590).

Sequence similarities

Belongs to the synuclein family.

Post-translational modifications

Phosphorylated, predominantly on serine residues. Phosphorylation by CK1 appears to occur on residues distinct from the residue phosphorylated by other kinases. Phosphorylation of Ser-129 is selective and extensive in synucleinopathy lesions. In vitro, phosphorylation at Ser-129 promoted insoluble fibril formation. Phosphorylated on Tyr-125 by a PTK2B-dependent pathway upon osmotic stress.. Hallmark lesions of neurodegenerative synucleinopathies contain alpha-synuclein that is modified by nitration of tyrosine residues and possibly by dityrosine cross-linking to generated stable oligomers.. Ubiquitinated. The predominant conjugate is the diubiquitinated form.. Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure.