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Article

Multiple phosphorylation of alpha-synuclein by protein tyrosine kinase Syk prevents eosin-induced aggregation.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology - 1 Feb 2002

Negro Alessandro, Brunati Anna Maria, Donella-Deana Arianna, Massimino Maria Lina, Pinna Lorenzo A

Abstract excerpt

The presence of aggregated alpha-synuclein molecules is a common denominator in a variety of neurodegenerative disorders. Here, we show that alpha-synuclein (alpha-syn) is an outstanding substrate for the protein tyrosine kinase p72syk (Syk), which phosphorylates three tyrosyl residues in its C-terminal domain (Y-125, Y-133, and Y-136), as revealed from experiments with mutants where these residues have been...

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Identifiers

PMID: 11744621
DOI: 10.1096/fj.01-0517fje

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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