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The extended PP1 toolkit: designed to create specificity
- Source :
-
Trends in Biochemical Sciences . Aug2010, Vol. 35 Issue 8, p450-458. 9p. - Publication Year :
- 2010
-
Abstract
- Protein Ser/Thr phosphatase-1 (PP1) catalyzes the majority of eukaryotic protein dephosphorylation reactions in a highly regulated and selective manner. Recent studies have identified an unusually diversified PP1 interactome with the properties of a regulatory toolkit. PP1-interacting proteins (PIPs) function as targeting subunits, substrates and/or inhibitors. As targeting subunits, PIPs contribute to substrate selection by bringing PP1 into the vicinity of specific substrates and by modulating substrate specificity via additional substrate docking sites or blocking substrate-binding channels. Many of the nearly 200 established mammalian PIPs are predicted to be intrinsically disordered, a property that facilitates their binding to a large surface area of PP1 via multiple docking motifs. These novel insights offer perspectives for the therapeutic targeting of PP1 by interfering with the binding of PIPs or substrates. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 09680004
- Volume :
- 35
- Issue :
- 8
- Database :
- Academic Search Index
- Journal :
- Trends in Biochemical Sciences
- Publication Type :
- Academic Journal
- Accession number :
- 52874956
- Full Text :
- https://doi.org/10.1016/j.tibs.2010.03.002