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  • Title: Superiority of PLK-2 as α-synuclein phosphorylating agent relies on unique specificity determinants.
    Author: Salvi M, Trashi E, Marin O, Negro A, Sarno S, Pinna LA.
    Journal: Biochem Biophys Res Commun; 2012 Feb 03; 418(1):156-60. PubMed ID: 22248692.
    Abstract:
    Phosphorylation of α-synuclein at Ser-129 is of crucial relevance to Parkinson's disease and related synucleinopathies. Here we provide biochemical evidence that PLK2 and to a lesser extent PLK3 are superior over CK2, as catalysts of Ser-129 phosphorylation both in full length α-synuclein and in a peptide reproducing the C-terminal segment of the protein. By using substituted peptides we also show that the sequence surrounding Ser-129 is optimally shaped for undergoing phosphorylation by PLK2, with special reference to the two acidic residues at positions n-3 (Glu-126) and n+2 (Glu-131) whose replacement with alanine abrogates phosphorylation.
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