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Review Article

Biogenesis and activity regulation of protein phosphatase 1

Iris Verbinnen, Monica Ferreira, Mathieu Bollen
Biochemical Society Transactions Feb 15, 2017, 45 (1) 89-99; DOI: 10.1042/BST20160154
Iris Verbinnen
Laboratory of Biosignaling & Therapeutics, KU Leuven Department of Cellular and Molecular Medicine, University of Leuven, B-3000 Leuven, Belgium
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Monica Ferreira
Laboratory of Biosignaling & Therapeutics, KU Leuven Department of Cellular and Molecular Medicine, University of Leuven, B-3000 Leuven, Belgium
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Mathieu Bollen
Laboratory of Biosignaling & Therapeutics, KU Leuven Department of Cellular and Molecular Medicine, University of Leuven, B-3000 Leuven, Belgium
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This article has a correction. Please see:

  • Correction: Biogenesis and activity regulation of protein phosphatase 1

Abstract

Protein 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. The diversity of PIPs is huge (≈200 in vertebrates), and most of them combine short linear motifs to form large and unique interaction interfaces with PP1. Many PIPs have separate domains for PP1 anchoring, PP1 regulation, substrate recruitment and subcellular targeting, which enable them to direct associated PP1 to a specific subset of substrates and mediate acute activity control. Hence, PP1 functions as the catalytic subunit of a large number of multimeric holoenzymes, each with its own subset of substrates and mechanism(s) of regulation.

  • dephosphorylation
  • enzyme regulation
  • PP1
  • Abbreviations

    FHA,
    ForkHead associated;
    PIPs,
    PP1-interacting proteins;
    PP1,
    protein phosphatase 1;
    PPP,
    phosphoprotein phosphatase;
    SKA,
    spindle- and kinetochore-associated;
    SLiMs,
    short linear motifs.
    • © 2017 The Author(s); published by Portland Press Limited on behalf of the Biochemical Society
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    February 2017

    Volume: 45 Issue: 1

    Biochemical Society Transactions: 45 (1)
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    Biogenesis and activity regulation of protein phosphatase 1
    Iris Verbinnen, Monica Ferreira, Mathieu Bollen
    Biochemical Society Transactions Feb 2017, 45 (1) 89-99; DOI: 10.1042/BST20160154
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    Biogenesis and activity regulation of protein phosphatase 1
    Iris Verbinnen, Monica Ferreira, Mathieu Bollen
    Biochemical Society Transactions Feb 2017, 45 (1) 89-99; DOI: 10.1042/BST20160154

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    • Article
      • Abstract
      • Introduction
      • PP1–PIP interaction modes
      • PIPs in the biogenesis and turnover of PP1
      • PIPs as substrate specifiers
      • Determinants of PP1 holoenzyme abundance
      • Acute activity regulation of PP1 holoenzymes
      • Conclusions
      • Competing Interests
      • References
    • Figures
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    Keywords

    dephosphorylation
    enzyme regulation
    PP1

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