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Protein phosphatase 2A: Variety of forms and diversity of functions
Author(s): Lechward K, Awotunde OS, Swiatek W, Muszynska G
Source: ACTA BIOCHIMICA POLONICA    Volume: 48    Issue: 4    Pages: 921-933    Published: 2001  
Times Cited: 73     References: 68     
Abstract: Protein phosphatase 2A (PP2A) comprises a diverse family of phosphoserine- and phosphothreonine-specific phosphatases present in all eukaryotic cells. All forms of PP2A contain a catalytic subunit (PP2Ac) which forms a stable complex with the structural subunit PR65/A. The heterodimer PP2Ac-PR65/A associates with regulatory proteins, termed variable subunits, in order to form trimeric holoenzymes attributed with distinct substrate specificity and targeted to different subcellular compartments. PP2Ac activity can be modulated by reversible phosphorylation on Tyr(307) an methylation on C-terminal Leu(309). Studies on PP2A have shown that this enzyme may be implicated in the regulation of metabolism, transcription, RNA splicing, translation, differentiation, cell cycle, oncogenic transformation and signal transduction.
Document Type: Review
Language: English
Reprint Address: Muszynska, G (reprint author), Polish Acad Sci, Inst Biochem & Biophys, A Pawinskiego 5A, PL-02106 Warsaw, Poland
Addresses:
1. Polish Acad Sci, Inst Biochem & Biophys, PL-02106 Warsaw, Poland
2. Med Univ Gdansk, Intercollegiate Fac Biotechnol, Cell & Mol Signaling Lab, Gdansk, Poland
Publisher: ACTA BIOCHIMICA POLONICA, PASTEURA 3, 02-093 WARSAW, POLAND
Subject Category: Biochemistry & Molecular Biology
IDS Number: 507WG
ISSN: 0001-527X
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