Protein phosphatase type 2C dephosphorylates BAD.
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. Ser(155) is involved in heterodimerization with Bcl-X(L). We could demonstrate that PP1, PP2A and PP2C act on this site in vitro. However, only PP2C gives priority to P-Ser(155) compared to P-Ser(112) and P-Ser(136) on BAD. The results indicate that PP2C is an additional factor triggering the pro-apoptotic function of BAD.
Klumpp
Susanne
S
Institut für Pharamzeutische und Medizinische Chemie, Westfälische Wilhelms-Universität, Hittorfstrasse 58-62, 48149 Münster, Germany. klumpp@uni-muenster.de
Selke
Dagmar
D
Krieglstein
Josef
J
D000595:Amino Acid Sequence; D002352:Carrier Proteins / Q000737:chemistry / Q000187:drug effects / Q000378:metabolism*; D010749:Phosphoprotein Phosphatases / Q000494:pharmacology*; D010766:Phosphorylation / Q000187:drug effects; D000071636:Protein Phosphatase 2C; D012694:Serine; D051025:bcl-Associated Death Protein
D002352:Carrier Proteins; D051025:bcl-Associated Death Protein; D012694:Serine; D010749:Phosphoprotein Phosphatases; D000071636:Protein Phosphatase 2C