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Res Lett Biochem. 2009;2009:685342. doi: 10.1155/2009/685342. Epub 2009 Jul 6.

Dephosphorylation of Centrins by Protein Phosphatase 2C α and β.

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Institut für Pharmazeutische und Medizinische Chemie, Westfälische Wilhelms-Universität Münster, Hittorfstr. 58-62, D-48149 Münster, Germany.


In the present study, we identified protein phosphatases dephosphorylating centrins previously phosphorylated by protein kinase CK2. The following phosphatases known to be present in the retina were tested: PP1, PP2A, PP2B, PP2C, PP5, and alkaline phosphatase. PP2C α and β were capable of dephosphorylating P-Thr(138)-centrin1 most efficiently. PP2Cδ was inactive and the other retinal phosphatases also had much less or no effect. Similar results were observed for centrins 2 and 4. Centrin3 was not a substrate for CK2. The results suggest PP2C α and β to play a significant role in regulating the phosphorylation status of centrins in vivo.

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