Reference : Recent insights into Protein Phosphatase 2A structure and regulation : The reason why PP...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/83895
Recent insights into Protein Phosphatase 2A structure and regulation : The reason why PP2A is no longer considered as a lazy passive housekeeping enzyme
English
Martin, Maud mailto [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie cell. et moléc. >]
Kettmann, Richard mailto [Université de Liège - ULg > Chimie et bio-industries > Centre de Bio. Fond. - Section de Biologie cell. et moléc. >]
Dequiedt, Franck mailto [Université de Liège - ULg > > GIGA-Research - Centre de Bio. Fond. - Section de Biologie cell. et moléc. >]
2010
Biotechnologie, Agronomie, Société et Environnement = Biotechnology, Agronomy, Society and Environment [=BASE]
Presses Agronomiques de Gembloux
14
1
243-252
Yes (verified by ORBi)
1370-6233
Gembloux
Belgique
[en] PP2A ; structure ; regulatory subunits
[en] Reversible protein phosphorylation is a major intracellular mechanism for controlling many important physiological activities. In the past, most of the attention was focused primarily on protein kinases and on their regulation, mainly because phosphatases were then viewed as simple housekeeping enzymes. But advances in the understanding of phosphatases make now clear that protein phosphatases are dynamic and highly regulated enzymes and are as important as kinases in the regulation of cellular processes involving protein phosphorylation.
Protein phosphatase 2A (PP2A) is a very abundant -it accounts for as much as 1% of total cellular protein-, ubiquitous and remarkably conserved enzyme. By dephosphorylating a plethora of cellular proteins, it is involved in the regulation of nearly all cellular activities.
http://hdl.handle.net/2268/83895

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