Results 281 to 290 of about 1,442,861 (307)
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Combinatorial control of protein phosphatase-1
Trends in Biochemical Sciences, 2001The catalytic subunit of the type 1 Ser/Thr protein phosphatases (PP1) can interact with many different regulatory (R) subunits. These R subunits function as activity-modulators, targeting subunits and/or substrates. The specificity of the R subunits can be accounted for by their interaction with specific subsets of binding pockets on the catalytic ...
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Interactor-Guided Dephosphorylation by Protein Phosphatase-1
2013Protein phosphatase-1 (PP1) is an essential enzyme for every eukaryotic cell and catalyzes more than half of all protein dephosphorylations at serine and threonine residues. The free catalytic subunit of PP1 shows little substrate selectivity but is tightly regulated in vivo by a large variety of structurally unrelated PP1-interacting proteins (PIPs ...
Shannah, Boens +3 more
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Biogenesis and activity regulation of protein phosphatase 1
Biochemical Society Transactions, 2017Protein phosphatase 1 (PP1) is expressed in all eukaryotic cells and catalyzes a substantial fraction of phosphoserine/threonine dephosphorylation reactions. It forms stable complexes with PP1-interacting proteins (PIPs) that guide the phosphatase throughout its life cycle and control its fate and function.
Iris, Verbinnen +2 more
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Preparation and Characterization of Recombinant Protein Phosphatase 1
2003Publisher Summary The chapter describes preparation and characterization of recombinant protein phosphatase 1 (PP1). Various methods for preparation of PP1C in bacteria, and methods for preparation of PP1C in Sf9 cells using the baculovirus expression system are presented. The chapter discusses the preparation of phosphorylated and thiophosphorylated
Takuo, Watanabe +7 more
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Regulation of Glycogen Synthase and Protein Phosphatase-1 by Hexosamines
Diabetes, 1996The hexosamine biosynthesis pathway has been hypothesized to be involved in mediating some of the adverse effects of high glucose. We have previously shown that glucose downregulates basal glycogen synthase (GS) activity in Rat-1 cells and that overexpressing the rate-limiting enzyme in the hexosamine biosynthesis pathway (glutamine:fructose-6 ...
E D, Crook, D A, McClain
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Identification of Cellular Protein Phosphatase-1 Regulators
2007Protein phosphatase-1 (PP1) is a major phosphoserine/phosphothreonine phosphatase that regulates multiple physiological events in all eukaryotic cells. Action of PP1 in cells is dictated by the association of PP1 catalytic subunit with one or more regulatory subunits that define both its catalytic function and subcellular localization.
David W, Roadcap +2 more
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Protein phosphatase 1 – targeted in many directions
Journal of Cell Science, 2002Protein phosphatase 1 (PP1) is a major eukaryotic protein serine/threonine phosphatase that regulates an enormous variety of cellular functions through the interaction of its catalytic subunit (PP1c) with over fifty different established or putative regulatory subunits.
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Protein phosphatase 1 is a key player in nuclear events
Cellular Signalling, 2015Reversible protein phosphorylation at serine (Ser), threonine (Thr) and tyrosine (Tyr) residues is among the major regulatory mechanism in eukaryotic cells. The eukaryotic genome encodes many protein kinases and protein phosphatases. However, the localization, activity and specificity towards phosphatase substrates are dictated by a large array of ...
Sandra, Rebelo +4 more
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Mutational Analysis of Substrate Recognition by Protein Phosphatase 1
Biochemistry, 1997The role of residues that are involved in substrate recognition by rabbit muscle protein phosphatase 1alpha (PP1) was investigated by site-directed mutagenesis and kinetic analyses using phosphorylase a, RII peptide, Kemptide, and p-nitrophenyl phosphate as substrates.
L, Zhang, E Y, Lee
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Carcinogenic Aspects of Protein Phosphatase 1 and 2A Inhibitors
2009Okadaic acid is functionally a potent tumor promoter working through inhibition of protein phosphatases 1 and 2A (PP1 and PP2A), resulting in sustained phosphorylation of proteins in cells. The mechanism of tumor promotion with okadaic acid is thus completely different from that of the classic tumor promoter phorbol ester.
Hirota, Fujiki, Masami, Suganuma
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