Dephosphorylation of Centrins by Protein Phosphatase 2C α and β

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 dephosphor...

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Bibliographic Details
Published in:Biochemistry Research International 2009-01, Vol.2009 (2009), p.1-4-004
Main Authors: Thissen, Marie-Christin, Krieglstein, Josef, Wolfrum, Uwe, Klumpp, Susanne
Format: Article
Language:English
Subjects:
Research Letter
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Summary: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-Thr138-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.
ISSN:2090-2247
1687-6709
1687-6717
DOI:10.1155/2009/685342