Department of Biological Chemistry and CNR Institute of Neurosciences, University of Padova, V.le G. Colombo 3, 35131 Padova, Italy.
Biochem Biophys Res Commun. 2012 Feb 3;418(1):156-60. doi: 10.1016/j.bbrc.2011.12.152. Epub 2012 Jan 10.
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.
α-突触核蛋白在丝氨酸 129 位的磷酸化与帕金森病和相关的突触核蛋白病有至关重要的关系。在这里，我们提供了生化证据，表明 PLK2 比 CK2 更能有效地催化全长α-突触核蛋白和复制蛋白质 C 末端片段的肽中的丝氨酸 129 位磷酸化，PLK3 的作用则较小。通过使用取代的肽，我们还表明，丝氨酸 129 周围的序列特别适合 PLK2 进行磷酸化，这与位置 n-3（Glu-126）和 n+2（Glu-131）的两个酸性残基有关，这两个酸性残基的替换会使磷酸化作用丧失。
