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Efficient Modification of Alpha-Synuclein Serine 129 by Protein Kinase CK1 Requires Phosphorylation of Tyrosine 125 as a Priming Event

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Kosten, Jonas | Binolfi, Andres | Stuiver, Marchel | Verzini, Silvia | Theillet, Francois-Xavier | Bekei, Beata | van Rossum, Marleen | Selenko, Philipp

Edité par CCSD ; American Chemical Society (ACS) -

International audience. S129-phosphorylated alpha-synuclein (α-syn) is abundantly found in Lewy-bodyinclusions of Parkinson’s disease patients. Residues neighboring S129 also include the α-syntyrosine phosphorylation sites Y125, Y133 and Y136. Here, we use time-resolved NMRspectroscopy to delineate atomic resolution insights into the modification behaviors ofdifferent serine and tyrosine kinases targeting these sites and show that Y125 phosphorylationconstitutes a necessary priming event for the efficient modification of S129 by Casein kinaseI, both in reconstituted kinase reactions and mammalian cell lysates. These results suggestthat α-syn Y125 phosphorylation augments S129 modification under physiological in vivoconditions.

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