The extended PP1 toolkit: designed to create specificity

By M. Bollen, W. Peti, M. Ragusa, M. Beullens. TIBS -Trends in Biochemical Sciences. Regular ed, 2010

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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.

Subfields: Molecular Biology

View Paper: https://www.semanticscholar.org/paper/01216a2968a08eadede7e37faf09f8d026dcc08a