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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Boknik, Peter Kristensen, Torsten König, Simone Kirchhefer, Uwe Müller, Frank U. Seidl, Matthias D. Heinick, Alexander |
| Description | Author Affiliation: Kirchhefer U ( From the Institut für Pharmakologie und Toxikologie, Universitätsklinikum Münster, 48149 Münster, Germany.) |
| Abstract | Protein phosphatase 2A (PP2A) is a family of multifunctional serine/threonine phosphatases consisting of a catalytic C, a structural A, and a regulatory B subunit. The substrate and therefore the functional specificity of PP2A are determined by the assembly of the enzyme complex with the appropriate regulatory B subunit families, namely B55, B56, PR72, or PR93/PR110. It has been suggested that additional levels of regulating PP2A function may result from the phosphorylation of B56 isoforms. In this study, we identified a novel phosphorylation site at Ser(41) of B56 . This phosphoamino acid residue was efficiently phosphorylated in vitro by PKC . We detected a 7-fold higher phosphorylation of B56 in failing human hearts compared with nonfailing hearts. Purified PP2A dimeric holoenzyme (subunits C and A) was able to dephosphorylate PKC -phosphorylated B56 . The potency of B56 for PP2A inhibition was markedly increased by PKC phosphorylation. PP2A activity was also reduced in HEK293 cells transfected with a B56 mutant, where serine 41 was replaced by aspartic acid, which mimics phosphorylation. More evidence for a functional role of PKC -dependent phosphorylation of B56 was derived from Fluo-4 fluorescence measurements in phenylephrine-stimulated Flp293 cells. The endoplasmic reticulum Ca(2+) release was increased by 23% by expression of the pseudophosphorylated form compared with wild-type B56 . Taken together, our results suggest that PKC can modify PP2A activity by phosphorylation of B56 at Ser(41). This interplay between PKC and PP2A represents a new mechanism to regulate important cellular functions like cellular Ca(2+) homeostasis. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 1 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-01-03 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Calcium Metabolism Endoplasmic Reticulum Homeostasis Physiology Protein Kinase C-alpha Protein Phosphatase 2 Adrenergic Alpha-1 Receptor Agonists Pharmacology Amino Acid Substitution Animals Genetics HEK293 Cells Drug Effects Mutation, Missense Phenylephrine Phosphorylation Serine Sf9 Cells Spodoptera Clinical Trial Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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