| Literature DB >> 14585537 |
Alphonse Garcia1, Xavier Cayla, Julien Guergnon, Frédéric Dessauge, Véronique Hospital, Maria Paz Rebollo, Aarne Fleischer, Angelita Rebollo.
Abstract
The reversible phosphorylation of proteins controlled by protein kinases and protein phosphatases is a major mechanism that regulates a wide variety of cellular processes. In contrast to C. elegans, recent studies in mammalian cells have highlighted a major role of serine/threonine protein phosphorylation in apoptosis. To illustrate the importance of dephosphorylation processes in apoptosis, this review will focus on recent studies suggesting that the interaction of the serine/threonine protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) with certain regulators of the Bcl-2 family is critically involved in the control of apoptosis.Entities:
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Year: 2003 PMID: 14585537 DOI: 10.1016/j.biochi.2003.09.004
Source DB: PubMed Journal: Biochimie ISSN: 0300-9084 Impact factor: 4.079