6533b859fe1ef96bd12b6e8d
RESEARCH PRODUCT
Dephosphorylation of Centrins by Protein Phosphatase 2C α and β.
Marie-christin ThissenJosef KrieglsteinUwe WolfrumSusanne Klumppsubject
PhosphatasePyruvate dehydrogenase phosphataseBioinformaticsDephosphorylationlcsh:Chemistrylcsh:QD241-441lcsh:Biochemistrychemistry.chemical_compoundlcsh:Organic chemistryIn vivoResearch LetterMedicinelcsh:QD415-436lcsh:Sciencelcsh:QH301-705.5Earth-Surface Processesbusiness.industryRetinalProtein phosphatase 2Biochemistrychemistrylcsh:Biology (General)lcsh:QD1-999embryonic structuresAlkaline phosphatasePhosphorylationlcsh:Qbusinessdescription
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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2009-03-26 | Research letters in biochemistry |