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Deputy Director of Department
Deputy Director of National Reference Center
Deputy Head of Facility
Director of Center
Director of Department
Director of Institute
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Group Leader
Head of Facility
Head of Operations
Head of Structure
Honorary President of the Departement
Labex Coordinator

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Chronic hepatitis associated with GB virus B persistence in a tamarin after intrahepatic inoculation of synthetic viral RNA

Two distinct coactivators, DRIP/mediator and SRC/p160, are differentially involved in vitamin D receptor transactivation during keratinocyte differentiation

© Research

Publication : Biochimie

Serine/threonine protein phosphatases PP1 and PP2A are key players in apoptosis

Team: Archived: Nuclear Magnetic Resonance Of Biomolecules

Member: Alphonse Garcia

Scientific Fields

Diseases

Organisms

Applications

Technique

Published in Biochimie - 01 Aug 2003

Garcia A, Cayla X, Guergnon J, Dessauge F, Hospital V, Rebollo MP, Fleischer A, Rebollo A

Link to Pubmed [PMID] – 14585537

Biochimie 2003 Aug;85(8):721-6

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.

Published on: 01 Aug 2003