Dephosphorylation of Centrins by Protein Phosphatase 2C α and β
Joint Authors
Klumpp, Susanne
Wolfrum, Uwe
Krieglstein, Josef
Thissen, Marie-Christin
Source
Research Letters in Biochemistry
Issue
Vol. 2009, Issue 2009 (31 Dec. 2009), pp.1-4, 4 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2009-07-06
Country of Publication
Egypt
No. of Pages
4
Main Subjects
Abstract EN
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.
American Psychological Association (APA)
Thissen, Marie-Christin& Krieglstein, Josef& Wolfrum, Uwe& Klumpp, Susanne. 2009. Dephosphorylation of Centrins by Protein Phosphatase 2C α and β. Research Letters in Biochemistry،Vol. 2009, no. 2009, pp.1-4.
https://search.emarefa.net/detail/BIM-490449
Modern Language Association (MLA)
Thissen, Marie-Christin…[et al.]. Dephosphorylation of Centrins by Protein Phosphatase 2C α and β. Research Letters in Biochemistry No. 2009 (2009), pp.1-4.
https://search.emarefa.net/detail/BIM-490449
American Medical Association (AMA)
Thissen, Marie-Christin& Krieglstein, Josef& Wolfrum, Uwe& Klumpp, Susanne. Dephosphorylation of Centrins by Protein Phosphatase 2C α and β. Research Letters in Biochemistry. 2009. Vol. 2009, no. 2009, pp.1-4.
https://search.emarefa.net/detail/BIM-490449
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-490449
