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Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
Author(s): Janssens V, Goris J
Source: BIOCHEMICAL JOURNAL    Volume: 353    Pages: 417-439    Part: Part 3    Published: FEB 1 2001  
Times Cited: 573     References: 341     
Abstract: Protein phosphatase 2A (PP2A) comprises a family of serine/threonine phosphatases, minimally containing a well conserved catalytic subunit, the activity of which is highly regulated. Regulation is accomplished mainly by members of a family of regulatory subunits, which determine the substrate specificity. (sub)cellular localization and catalytic activity of the PP2A holoenzymes. Moreover, the catalytic subunit is subject to two types of post-translational modification, phosphorylation and methylation, which are also thought to be important regulatory devices, The regulatory ability of PTPA (PTPase activator), originally identified as a protein stimulating the phosphotyrosine phosphatase activity of PP2A, will also be discussed, alongside the other regulatory inputs. The use of specific PP2A inhibitors and molecular genetics in yeast, Drosophila and mice has revealed roles for PP2A in cell cycle regulation, cell morphology and development, PP2A also plays a prominent role in the regulation of specific signal transduction cascades, as witnessed by its presence in a number of macromolecular signalling modules, where it is often found in association with other phosphatases and kinases. Additionally, PP2A interacts with a substantial number of other cellular and viral proteins. which are PP2A substrates, target PP2A to different subcellular compartments or affect enzyme activity. Finally, the de-regulation of PP2A in some specific pathologies will be touched upon.
Document Type: Review
Language: English
Reprint Address: Goris, J (reprint author), Catholic Univ Louvain, Afdeling Biochem, Fac Geneeskunde, Herestr 49, B-3000 Louvain, Belgium
Addresses:
1. Catholic Univ Louvain, Afdeling Biochem, Fac Geneeskunde, B-3000 Louvain, Belgium
Publisher: PORTLAND PRESS, 59 PORTLAND PLACE, LONDON W1N 3AJ, ENGLAND
Subject Category: Biochemistry & Molecular Biology
IDS Number: 401RJ
ISSN: 0264-6021
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