Phosphorylation of bid by casein kinases I and II regulates its cleavage by caspase 8 |
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Authors: | Desagher S Osen-Sand A Montessuit S Magnenat E Vilbois F Hochmann A Journot L Antonsson B Martinou J C |
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Affiliation: | CNRS UPR 9023, Montpellier, France. desagher@montp.inserm.fr |
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Abstract: | Bid plays an essential role in Fas-mediated apoptosis of the so-called type II cells. In these cells, following cleavage by caspase 8, the C-terminal fragment of Bid translocates to mitochondria and triggers the release of apoptogenic factors, thereby inducing cell death. Here we report that Bid is phosphorylated by casein kinase I (CKI) and casein kinase II (CKII). Inhibition of CKI and CKII accelerated Fas-mediated apoptosis and Bid cleavage, whereas hyperactivity of the kinases delayed apoptosis. When phosphorylated, Bid was insensitive to caspase 8 cleavage in vitro. Moreover, a mutant of Bid that cannot be phosphorylated was found to be more toxic than wild-type Bid. Together, these data indicate that phosphorylation of Bid represents a new mechanism whereby cells control apoptosis. |
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