Literature DB >> 12590938

Protein phosphatase type 2C dephosphorylates BAD.

Susanne Klumpp1, Dagmar Selke, Josef Krieglstein.   

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. 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.

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Year:  2003        PMID： 12590938     DOI： 10.1016/s0197-0186(02)00174-2

Source DB:  PubMed          Journal:  Neurochem Int        ISSN： 0197-0186            Impact factor:   3.921


  16 in total

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