journal article Feb 08, 2017

Biogenesis and activity regulation of protein phosphatase 1

View at Publisher Save 10.1042/bst20160154
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.
Topics

No keywords indexed for this article. Browse by subject →

References
70
[1]
Bollen "The extended PP1 toolkit: designed to create specificity" Trends Biochem. Sci. (2010) 10.1016/j.tibs.2010.03.002
[2]
Choy "Regulation of protein phosphatase 1 by intrinsically disordered proteins" Biochem. Soc. Trans. (2012) 10.1042/bst20120094
[3]
The PP1 binding code: a molecular‐lego strategy that governs specificity

Ewald Heroes, Bart Lesage, Janina Görnemann et al.

The FEBS Journal 2013 10.1111/j.1742-4658.2012.08547.x
[4]
Lad "The rate of hydrolysis of phosphomonoester dianions and the exceptional catalytic proficiencies of protein and inositol phosphatases" Proc. Natl Acad. Sci. U.S.A. (2003) 10.1073/pnas.0631607100
[5]
Gibbons "Expression of human protein phosphatase-1 in Saccharomyces cerevisiae highlights the role of phosphatase isoforms in regulating eukaryotic functions" J. Biol. Chem. (2007) 10.1074/jbc.m701272200
[6]
Lundberg "Defining the transcriptome and proteome in three functionally different human cell lines" Mol. Syst. Biol. (2010) 10.1038/msb.2010.106
[7]
Nagaraj "Deep proteome and transcriptome mapping of a human cancer cell line" Mol. Syst. Biol. (2011) 10.1038/msb.2011.81
[8]
Ceulemans "Functional diversity of protein phosphatase-1, a cellular economizer and reset button" Physiol. Rev. (2004) 10.1152/physrev.00013.2003
[9]
Oberoi "Structural and functional basis of protein phosphatase 5 substrate specificity" Proc. Natl Acad. Sci. U.S.A. (2016) 10.1073/pnas.1603059113
[10]
Chatterjee "Development of a peptide that selectively activates protein phosphatase-1 in living cells" Angew. Chem. Int. Ed. (2012) 10.1002/anie.201204308
[11]
Terrak "Structural basis of protein phosphatase 1 regulation" Nature (2004) 10.1038/nature02582
[12]
Ragusa "Spinophilin directs protein phosphatase 1 specificity by blocking substrate binding sites" Nat. Struct. Mol. Biol. (2010) 10.1038/nsmb.1786
[13]
O'Connell "The molecular basis for substrate specificity of the nuclear NIPP1:PP1 holoenzyme" Structure (2012) 10.1016/j.str.2012.08.003
[14]
Choy "Understanding the antagonism of retinoblastoma protein dephosphorylation by PNUTS provides insights into the PP1 regulatory code" Proc. Natl Acad. Sci. U.S.A. (2014) 10.1073/pnas.1317395111
[15]
Choy "Structural and functional analysis of the GADD34:PP1 eIF2α phosphatase" Cell Rep. (2015) 10.1016/j.celrep.2015.05.043
[16]
Kumar "The Ki-67 and RepoMan mitotic phosphatases assemble via an identical, yet novel mechanism" eLife (2016) 10.7554/elife.16539
[17]
Bollen "Combinatorial control of protein phosphatase-1" Trends Biochem. Sci. (2001) 10.1016/s0968-0004(01)01836-9
[18]
Endo "Multiple structural elements define the specificity of recombinant human inhibitor-1 as a protein phosphatase-1 inhibitor" Biochemistry (1996) 10.1021/bi952940f
[19]
Beullens "The C-terminus of NIPP1 (nuclear inhibitor of protein phosphatase-1) contains a novel binding site for protein phosphatase-1 that is controlled by tyrosine phosphorylation and RNA binding" Biochem. J. (2000) 10.1042/bj3520651
[20]
Ceulemans "Binding of the concave surface of the Sds22 superhelix to the α4/α5/α6-triangle of protein phosphatase-1" J. Biol. Chem. (2002) 10.1074/jbc.m206838200
[21]
Heroes "Metals in the active site of native protein phosphatase-1" J. Inorg. Biochem. (2015) 10.1016/j.jinorgbio.2015.03.012
[22]
Bollen "The structure, role, and regulation of type 1 protein phosphatases" Crit. Rev. Biochem. Mol. Biol. (1992) 10.3109/10409239209082564
[23]
Cheng "Assembly and quality control of the protein phosphatase 1 holoenzyme involves the Cdc48-Shp1 chaperone" J. Cell Sci. (2015) 10.1242/jcs.165159
[24]
Lesage "A complex of catalytically inactive protein phosphatase-1 sandwiched between Sds22 and inhibitor-3" Biochemistry (2007) 10.1021/bi7003119
[25]
Pedelini "YPI1 and SDS22 proteins regulate the nuclear localization and function of yeast type 1 phosphatase Glc7" J. Biol. Chem. (2007) 10.1074/jbc.m607171200
[26]
Eiteneuer "Inhibitor-3 ensures bipolar mitotic spindle attachment by limiting association of SDS22 with kinetochore-bound protein phosphatase-1" EMBO J. (2014) 10.15252/embj.201489054
[27]
Structural Basis for Regulation of Protein Phosphatase 1 by Inhibitor-2

Thomas D. Hurley, Jie Yang, Lili Zhang et al.

Journal of Biological Chemistry 2007 10.1074/jbc.m703472200
[28]
Ceulemans "Regulator-driven functional diversification of protein phosphatase-1 in eukaryotic evolution" BioEssays (2002) 10.1002/bies.10069
[29]
Smetana "Interaction analysis of the heterotrimer formed by the phosphatase 2A catalytic subunit, α4 and the mammalian ortholog of yeast Tip41 (TIPRL)" FEBS J. (2007) 10.1111/j.1742-4658.2007.06112.x
[30]
Sents "The biogenesis of active protein phosphatase 2A holoenzymes: a tightly regulated process creating phosphatase specificity" FEBS J. (2013) 10.1111/j.1742-4658.2012.08579.x
[31]
Jiang "Structural basis of protein phosphatase 2A stable latency" Nat. Commun. (2013) 10.1038/ncomms2663
[32]
Crystal structure of the human Tip41 orthologue, TIPRL, reveals a novel fold and a binding site for the PP2Ac C-terminus

Valéria Scorsato, Tatiani B. Lima, Germanna L. Righetto et al.

Scientific Reports 2016 10.1038/srep30813
[33]
Guo "Structural basis of PP2A activation by PTPA, an ATP-dependent activation chaperone" Cell Res. (2014) 10.1038/cr.2013.138
[34]
Khromov "Phosphorylation-dependent autoinhibition of myosin light chain phosphatase accounts for Ca2+ sensitization force of smooth muscle contraction" J. Biol. Chem. (2009) 10.1074/jbc.m109.019729
[35]
Matsuzawa "Phospho-pivot modeling predicts specific interactions of protein phosphatase-1 with a phospho-inhibitor protein CPI-17" J. Biochem. (2005) 10.1093/jb/mvi077
[36]
An eIF2α-binding motif in protein phosphatase 1 subunit GADD34 and its viral orthologs is required to promote dephosphorylation of eIF2α

Margarito Rojas, Gabriel Vasconcelos, Thomas E. Dever

Proceedings of the National Academy of Sciences 2015 10.1073/pnas.1501557112
[37]
Jagiello (2000)
[38]
Zhou "Association with endoplasmic reticulum promotes proteasomal degradation of GADD34 protein" J. Biol. Chem. (2011) 10.1074/jbc.m110.212787
[39]
Trinkle-Mulcahy "Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cells" J. Cell Sci. (2001) 10.1242/jcs.114.23.4219
[40]
Hendrickx "Docking motif-guided mapping of the interactome of protein phosphatase-1" Chem. Biol. (2009) 10.1016/j.chembiol.2009.02.012
[41]
Winkler "The selective inhibition of protein phosphatase-1 results in mitotic catastrophe and impaired tumor growth" J. Cell Sci. (2015) 10.1242/jcs.175588
[42]
Antagonism of the Phosphatase PP1 by the Measles Virus V Protein Is Required for Innate Immune Escape of MDA5

Meredith E. Davis, May K. Wang, Linda J. Rennick et al.

Cell Host & Microbe 2014 10.1016/j.chom.2014.06.007
[43]
Wu "Integration of Hippo signalling and the unfolded protein response to restrain liver overgrowth and tumorigenesis" Nat. Commun. (2015) 10.1038/ncomms7239
[44]
Hirschi "An overlapping kinase and phosphatase docking site regulates activity of the retinoblastoma protein" Nat. Struct. Mol. Biol. (2010) 10.1038/nsmb.1868
[45]
Ma "Dissociation of SHP-1 from spinophilin during platelet activation exposes an inhibitory binding site for protein phosphatase-1 (PP1)" PLoS ONE (2015) 10.1371/journal.pone.0119496
[46]
Dohadwala "Phosphorylation and inactivation of protein phosphatase 1 by cyclin-dependent kinases" Proc. Natl Acad. Sci U.S.A. (1994) 10.1073/pnas.91.14.6408
[47]
Nigavekar "Glc8 is a glucose-repressible activator of Glc7 protein phosphatase-1" Arch. Biochem. Biophys. (2002) 10.1016/s0003-9861(02)00231-x
[48]
Kelsall "R3f, a novel membrane-associated glycogen targeting subunit of protein phosphatase 1 regulates glycogen synthase in astrocytoma cells in response to glucose and extracellular signals" J. Neurochem. (2011) 10.1111/j.1471-4159.2011.07345.x
[49]
Fisher "Phosphatase 1 nuclear targeting subunit is an essential regulator of M-phase entry, maintenance, and exit" J. Biol. Chem. (2014) 10.1074/jbc.m114.572149
[50]
Huang "Protein phosphatase-1 inhibitor-3 is an in vivo target of caspase-3 and participates in the apoptotic response" J. Biol. Chem. (2008) 10.1074/jbc.m709735200

Showing 50 of 70 references

Metrics
94
Citations
70
References
Details
Published
Feb 08, 2017
Vol/Issue
45(1)
Pages
89-99
Cite This Article
Iris Verbinnen, Mónica Ferreira, Mathieu Bollen (2017). Biogenesis and activity regulation of protein phosphatase 1. Biochemical Society Transactions, 45(1), 89-99. https://doi.org/10.1042/bst20160154