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Protein phosphatase type 2C dephosphorylates BAD |
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| Authors: | Klumpp Susanne Selke Dagmar Krieglstein Josef |
| Institution: | a Institut für Pharamzeutische und Medizinische Chemie, Westfälische Wilhelms-Universität, Hittorfstrasse 58-62, Münster 48149, Germany b Institut für Pharmakologie und Toxikologie, Fachbereich Pharmazie, Philipps-Universität, Marburg, Germany |
| Abstract: | Reversible phosphorylation modulates a cells’ susceptibility to apoptosis. The phosphorylation status of BAD, a member of the Bcl-2 protein family, is an important checkpoint governing life-or-death decisions: Phosphorylation of serine residues 112, 136 and 155 on BAD prevents apoptosis. Here we report that BAD is a substrate for PP2C. Ser155 is involved in heterodimerization with Bcl-XL. We could demonstrate that PP1, PP2A and PP2C act on this site in vitro. However, only PP2C gives priority to P-Ser155 compared to P-Ser112 and P-Ser136 on BAD. The results indicate that PP2C is an additional factor triggering the pro-apoptotic function of BAD. |
| Keywords: | Apoptosis BAD Dephosphorylation Phosphatases Phosphorylation PP2C |
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