Regulation of protein phosphatase-1

Chemistry and Biology

Volumn 7, Issue 1, 2000, Pages

  Aggen, James B ^a   Nairn, Angus C ^b   Chamberlin, Richard ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b ROCKEFELLER UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA;

EID: 0034009287     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(00)00069-7     Document Type: Review

References (87)

1. Magee A.I. Cell adhesion molecules and intracellular signalling: from fly to man. Cell. Signal. 7:1995;165-170.
2. Hunter T. Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signalling. Cell. 80:1995;225-236.
3. Cohen P.T.W. Novel protein serine/threonine phosphatases: variety is the spice of life. Trends Biochem. Sci. 22:1997;245-251.
4. Shenolikar S., Nairn A.C. Protein phosphatases: recent progress. Adv. Second Messenger Phosphoprotein Res. 23:1991;1-121.
5. Pinna L.A., Ruzzene M. How do protein kinases recognize their substrates? Biochim. Biophys. Acta. 1314:1996;191-225.
6. Pinna L.A., Donella-Deana A. Phosphorylated synthetic peptides as tools for studying protein phosphatases. Biochim. Biophys. Acta. 1222:1994;415-431.
7. Wera S., Hemmings B.A. Serine/threonine protein phosphatases. Biochem. J. 311:1995;17-29.
8. Cohen P. The structure and regulation of protein phosphatases. Annu. Rev. Biochem. 58:1989;453-508.
9. Feng Z.H., Wilson S.E., Peng Z.Y., Schlender K.K., Reimann E.M., Trumbly R.J. The yeast GLC7 gene required for glycogen accumulation encodes a type 1 protein phosphatase. J. Biol. Chem. 266:1991;23796-23801.
10. Stuart J.S., Frederick D.L., Varner C.M., Tatchell K. The mutant type 1 protein phosphatase encoded by glc7-1 from Saccharomyces cerevisiae fails to interact productively with the GAC1-encoded regulatory subunit. Mol. Cell. Biol. 14:1994;896-905.
11. Cohen P. Classification of protein-serine/threonine phosphatases: identification and quantitation in cell extracts. Methods Enzymol. 201:1991;389-427.
12. Murata K., Wu J., Brautigan D.L. B cell receptor-associated protein α4 displays rapamycin-sensitive binding directly to the catalytic subunit of protein phosphatase 2A. Proc. Natl Acad. Sci. USA. 94:1997;10624-10629.
13. Doherty M.J., Moorhead G., Morrice N., Cohen P., Cohen P.T.W. Amino acid sequence and expression of the hepatic glycogen-binding (GL)-subunit of protein phosphatase-1. FEBS Lett. 375:1995;294-298.
14. Endo S., Zhou X., Connor J., Wang B., Shenolikar S. Multiple structural elements define the specificity of recombinant human inhibitor-1 as a protein phosphatase-1 inhibitor. Biochemistry. 35:1996;5220-5228.
15. Johnson D.F., Cohen P.T.W.et al. Identification of protein-phosphatase-1-binding domains on the glycogen and myofibrillar targeting subunits. Eur. J. Biochem. 239:1996;317-325.
16. Tanaka J., Nakano T.et al. Interaction of myosin phosphatase target subunit 1 with the catalytic subunit of type 1 protein phosphatase. Biochemistry. 37:1998;16697-16703.
17. Huang H.-B., Nairn A.C.et al. Characterization of the inhibition of protein phosphatase-1 by DARPP-32 and inhibitor-2. J. Biol. Chem. 274:1999;7870-7878.
18. Kwon Y.-G., Huang H.-B., Desdouits F., Girault J.-A., Greengard P., Nairn A.C. Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins. Proc. Natl Acad. Sci. USA. 94:1997;3536-3541.
19. Zhao S., Lee E.Y.C. A protein phosphatase-1-binding motif identified by the panning of a random peptide display library. J. Biol. Chem. 272:1997;28368-28372.
20. Egloff M.-P., Johnson D.F., Moorhead G., Cohen P.T.W., Cohen P., Barford D. Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1. EMBO J. 16:1997;1876-1887.
21. Goldberg J., Huang H.B., Kwon Y.G., Greengard P., Nairn A.C., Kuriyan J. Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature. 376:1995;745-753.
22. Egloff M., Cohen P.T.W., Reinemer P., Barford D. Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate. J. Mol. Biol. 254:1995;942-959.
23. Stralfors P., Hiraga A., Cohen P. The protein phosphatases involved in cellular regulation. Purification and characterisation of the glycogen-bound form of protein phosphatase-1 from rabbit skeletal muscle. Eur. J. Biochem. 149:1985;295.
24. Hiraga A., Cohen P. Phosphorylation of the glycogen-binding subunit of protein phosphatase-1G by cyclic-AMP-dependent protein kinase promotes translocation of the phosphatase from glycogen to cytosol in rabbit skeletal muscle. Eur. J. Biochem. 161:1986;763-769.
25. Hubbard M.J., Dent P., Smythe C., Cohen P. Targeting of protein phosphatase 1 to the sarcoplasmic reticulum of rabbit skeletal muscle by a protein that is very similar or identical to the G subunit that directs the enzyme to glycogen. Eur. J. Biochem. 189:1990;243-249.
26. Hubbard M.J., Cohen P. Regulation of protein phosphatase-1G from rabbit skeletal muscle. 2. Catalytic subunit translocation is a mechanism for reversible inhibition of activity toward glycogen-bound substrates. Eur. J. Biochem. 186:1989;711-716.
27. Stralfors P. The protein phosphatases involved in cellular regulation. Purification and characterisation of the glycogen-bound form of protein phosphatase-1 from rabbit skeletal muscle. Eur. J. Biochem. 149:1985;295-303.
28. Hubbard M.J., Cohen P. On target with a new mechanism for the regulation of protein phosphorylation. Trends Biochem. Sci. 18:1993;172-177.
29. MacKintosh C., Campbell D.G., Hiraga A., Cohen P. Phosphorylation of the glycogen-binding subunit of protein phosphatase-1G in response to adrenalin. FEBS Lett. 234:1988;189-194.
30. Hubbard M.J., Cohen P. Regulation of protein phosphatase-1G from rabbit skeletal muscle. 1. Phosphorylation by cAMP-dependent protein kinase at site 2 releases catalytic subunit from the glycogen-bound holoenzyme. Eur. J. Biochem. 186:1989;701-709.
31. Dent P., Lavoinne A., Nakielny S., Caudwell F.B., Watt P., Cohen P. The molecular mechanism by which insulin stimulates glycogen synthesis in mammalian skeletal muscle. Nature. 348:1990;302-308.
32. Srinivasan M., Begum N. Regulation of protein phosphatase 1 and 2A activities by insulin during myogenesis in rat skeletal muscle cells in culture. J. Biol. Chem. 269:1994;12514-12520.
33. Lavoinne A., Erikson E., Maller J.L., Price D.J., Avruch J., Cohen P. Purification and characterisation of the insulin-stimulated protein kinase from rabbit skeletal muscle; close similarity to S6 kinase II. Eur. J. Biochem. 199:1991;723-728.
34. Wu J., Kleiner U., Brautigan D.L. Protein phosphatase type-1 and glycogen bind to a domain in the skeletal muscle regulatory subunit containing conserved hydrophobic sequence motif. Biochemistry. 35:1996;13858-13864.
35. Printen J.A., Brady M.J., Saltiel A.R. PTG, a protein phosphatase 1 binding protein with a role in glycogen metabolism. Science. 275:1997;1475-1478.
36. Brady M.J., Printen J.A., Mastick C.C., Saltiel A.R. Role of protein targeting to glycogen (PTG) in the regulation of PP1 activity. J. Biol. Chem. 272:1997;20198-20204.
37. Brady M.J., Nairn A.C., Saltiel A.R. The regulation of glycogen synthase by protein phosphatase 1 in 3T3-L1 adipocytes. Evidence for a potential role for DARPP-32 in insulin action. J. Biol. Chem. 272:1997;29698-29703.
38. Murata K., Hirano K., Villa-Moruzzi E., Hartshorne D.J., Brautigan D.L. Differential localization of myosin and myosin phosphatase subunits in smooth muscle cells and migrating fibroblasts. Mol. Biol. Cell. 8:1997;663-673.
39. Takahashi N., Takemura K.et al. Localization of the gene coding for myosin phosphatase, target subunit 1 (MYPT1) to human chromosome 12q15-q21. Genomics. 44:1997;150-152.
40. Sobieszek A., Borkowski J., Babiychuk V.S. Purification and characterization of a smooth muscle myosin light chain kinase-phosphatase complex. J. Biol. Chem. 272:1997;7034-7041.
41. Inagaki N., Inagaki M.et al. Myosin binding subunit of smooth muscle myosin phosphatase at the cell-cell adhesion sites in MDCK cells. Biochem. Biophys. Res. Commun. 230:1997;552-556.
42. Hartshorne D.J., Ito M., Erdodi F. Myosin light chain phosphatase: subunit composition, interactions and regulation. J. Muscle Res. Cell Motility. 19:1998;325-341.
43. Hirano K., Phan B.C., Hartshorne D.J. Interactions of the subunits of smooth muscle myosin phosphatase. J. Biol. Chem. 272:1997;3683-3688.
44. Nakai K., Nishikawa M.et al. Regulation of myosin phosphatase through phosphorylation of the myosin-binding subunit in platelet activation. Blood. 90:1997;3936-3942.
45. Fuijoka M., Ito M.et al. A new isoform of human myosin phosphatase targeting/regulatory subunit (MYPT2): cDNA cloning, tissue expression, and chromosomal mapping. Genomics. 49:1998;59-68.
46. Van Eynde A., Bollen M.et al. Molecular cloning of NIPP-1, a nuclear inhibitor of protein phosphatase-1, reveals homology with polypeptides involved in RNA processing. J. Biol. Chem. 270:1995;28068-28074.
47. Allen P.B., Kwon Y.-G., Nairn A.C., Greengard P. Isolation and characterization of PNUTS, a putative PP1 nuclear targeting subunit. J. Biol. Chem. 273:1998;4089-4095.
48. Jagiello I., Bollen M.et al. NIPP-1, a nuclear inhibitory subunit of protein phosphatase-1, has RNA-binding properties. J. Biol. Chem. 272:1997;22067-22071.
49. Beullens M., Van Eynde A., Bollen M., Stalmans W. Inactivation of nuclear inhibitory polypeptides of protein phosphatase-1 (NIPP-1) by protein kinase A. J. Biol. Chem. 268:1993;13172-13177.
50. Vulsteke V., Beullens M., Waelkens E., Stalmans W., Bollen M. Properties and phosphorylation sites of baculovirus-expressed nuclear inhibitor of protein phosphatase-1 (NIPP-1). J. Biol. Chem. 272:1997;32972-32978.
51. Jagiello I., Buellens M., Stalmans W., Bollen M. Subunit structure and regulation of protein phosphatase-1 in rat liver nuclei. J. Biol. Chem. 270:1995;17257-17263.
52. Nimmo G.A., Cohen P. The regulation of glycogen metabolism. Purification and characterisation of protein phosphatase inhibitor-1 from rabbit skeletal muscle. Eur. J. Biochem. 87:1978;341-351.
53. Hemmings H.C.J., Girault J.-A., Nairn A.C., Bertuzzi G., Greengard P. Distribution of protein phosphatase inhibitor-1 in brain and peripheral tissues of various species: comparison with DARPP-32. J. Neurochem. 59:1992;1053-1061.
54. Matovcik L.M., Hemmings H.C.J., Kinder B.K. DARPP-32 (dopamine and cAMP-regulated phosphoprotein, M(r) 32,000) is a membrane protein in the bovine parathyroid. FEBS Lett. 364:1995;67-74.
55. Cohen P., Nimmo G.A. The purification and characterization of protein phosphatase inhibitor-1 from rabbit skeletal muscle. Biochem. Soc. Trans. 6:1978;17-20.
56. Aitken A., Bilham T., Cohen P. Complete primary structure of protein phosphatase inhibitor-1 from rabbit skeletal muscle. Eur. J. Biochem. 126:1982;235-246.
57. Williams K.R., Hemmings H.C. Jr., LoPresti M.B., Konigsberg W.H., Greengard P. DARPP-32, a dopamine- and cyclic AMP-regulated neuronal phosphoprotein. Primary structure and homology with protein phosphatase inhibitor-1. J. Biol. Chem. 261:1986;1890-1903.
58. Desdouits F., Girault J.-A.et al. Mechanism of inhibition of protein phosphatase 1 by DARPP-32: studies with recombinant DARPP-32 and synthetic peptides. Biochem. Biophys. Res. Commun. 206:1995;652-658.
59. Cohen P., Rylatt D.B., Nimmo G.A. The hormonal control of glycogen metabolism: the amino acid sequence at the phosphorylation site of protein phosphatase inhibitor-1. FEBS Lett. 76:1977;182-186.
60. Hemmings H.C.J., Greengard P., Tung H.Y.L., Cohen P. DARPP-32, a dopamine-regulated neuronal phosphoprotein, is a potent inhibitor of protein phosphatase-1. Nature. 310:1984;503-505.
61. Foulkes J.G., Strada S.J., Henderson P.J.F., Cohen P. A kinetic analysis of the effects of inhibitor-1 and inhibitor-2 on the activity of protein phosphatase-1. Eur. J. Biochem. 132:1983;309-313.
62. Hemmings H.C.J., Nairn A.C., Elliott J.I., Greengard P. Synthetic peptide analogs of DARPP-32 (Mr 32,000 dopamine- and cAMP-regulated phosphoprotein), an inhibitor of protein phosphatase-1. Phosphorylation, dephosphorylation, and inhibitory activity. J. Biol. Chem. 265:1990;20369-20376.
63. Aitken A., Cohen P. Isolation and characterization of active fragments of protein phosphatase inhibitor-1 from rabbit skeletal muscle. FEBS Lett. 147:1982;54-58.
64. Greengard P., Nishi A.et al. The DARPP-32/protein phosphatase-1 cascade: a model for signal integration. Brain Res. Rev. 26:1998;274-284.
65. Greengard P., Allen P.B., Nairn A.C. Beyond the dopamine receptor: the DARPP-32/protein phosphatase-1 cascade. Neuron. 23:1999;435-447.
66. Girault J.-A. Protein phosphorylation and dephosphorylation in mammalian central nervous system. Neurochem. Int. 23:1993;1-25.
67. Halpain S., Girault J.-A., Greengard P. Activation of NMDA receptors induces dephosphorylation of DARPP-32 in rat striatal slices. Nature. 343:1990;369-372.
68. Hemmings H.C.J., Nairn A.C., Greengard P. DARPP-32, a dopamine- and adenosine 3′:5′-monophosphate-regulated neuronal phosphoprotein. II. Comparison of the kinetics of phosphorylation of DARPP-32 and phosphatase inhibitor 1. J. Biol. Chem. 259:1984;14491-14497.
69. Nishi A., Snyder G.L., Nairn A.C., Greengard P. Role of calcineurin and protein phosphatase-2A in the regulation of DARPP-32 dephosphorylation in neostriatal neurons. J. Neurochem. 72:1999;2015-2021.
70. Bibb J.A., Greengard P.et al. Cdk5 phosphorylation of DARPP-32 modulates dopamine signaling in neurons. Nature. 402:1999;669-672.
71. Desdouits F., Cohen D., Nairn A.C., Greengard P., Girault J.-A. Phosphorylation of DARPP-32, a dopamine- and cAMP-regulated phosphoprotein, by casein kinase I in vitro and in vivo. J. Biol. Chem. 270:1995;8772-8778.
72. Girault J., Hemmings H.C.J., Williams K.R., Nairn A.C., Greengard P. Phosphorylation of DARPP-32, a dopamine- and cAMP-regulated phosphoprotein, by casein kinase II. J. Biol. Chem. 264:1989;21748-21759.
73. Desdouits F., Siciliano J.C., Greengard P., Girault J.-A. Dopamine- and cAMP-regulated phosphoprotein DARPP-32: phosphorylation of Ser-137 by casein kinase I inhibits dephosphorylation of Thr-34 by calcineurin. Proc. Natl Acad. Sci. USA. 92:1995;2682-2685.
74. Desdouits F., Siciliano J.C., Nairn A.C., Greengard P., Girault J.-A. Dephosphorylation of Ser-137 in DARPP-32 by protein phosphatases 2A and 2C: different roles in vitro and in striatonigral neurons. Biochem. J. 330:1998;211-216.
75. Huang F.L., Glinsmann W.H. Separation and characterization of two phosphorylase phosphatase inhibitors from rabbit skeletal muscle. Eur. J. Biochem. 70:1976;419-426.
76. Merlevede W., Vandenheede J.R., Goris J., Yang S.D. Regulation of ATP-Mg-dependent protein phosphatase. Curr. Top. Cell. Regul. 23:1984;177-215.
77. Picking W.D., DePaoli-Roach A.A.et al. Fluorescence studies on the interaction of inhibitor 2 and okadaic acid with the catalytic subunit of type 1 phosphoprotein phosphatases. Biochemistry. 30:1991;10280-10287.
78. Yang S.D., Vandenheede J.R., Merlevede W.R. Identification of inhibitor-2 as the ATP-mg-dependent protein phosphatase modulator. J. Biol. Chem. 256:1981;10231-10234.
79. Bollen M., DePaoli-Roach A.A., Stalmans W. Native cytosolic protein phosphatase-1 (PP-1S) containing modulator (inhibitor-2) is an active enzyme. FEBS Lett. 344:1994;196-200.
80. DePaoli-Roach A.A. Synergistic phosphorylation and activation of ATP-Mg-dependent phosphoprotein phosphatase by F A/GSK-3 and casein kinase II (PC0.7). J. Biol. Chem. 259:1984;12144-12152.
81. Holmes C.F.B., Kuret J., Chisholm A.A.K., Cohen P. Identification of the sites on rabbit skeletal muscle protein phosphatase inhibitor-2 phosphorylated by casein kinase-II. Biochim. Biophys. Acta. 870:1986;408-416.
82. Holmes C.F.B., Tonks N.K., Major H., Cohen P. Analysis of the in vivo phosphorylation state of protein phosphatase inhibitor-2 from rabbit skeletal muscle by fast-atom bombardment mass spectrometry. Biochim. Biophys. Acta. 929:1987;209-219.
83. Kakinoki Y., Somers J., Brautigan D.L. Multisite phosphorylation and the nuclear localization of phosphatase inhibitor 2-green fluorescent protein fusion protein during S phase of the cell growth cycle. J. Biol. Chem. 272:1997;32308-32314.
84. Park I.K., Roach P., Bondor J., Fow S.P., DePaoli-Roach A.A. Molecular mechanism of the synergistic phosphorylation of phosphatase inhibitor-2. Cloning, expression, and site-directed mutagenesis of inhibitor-2. J. Biol. Chem. 269:1994;944-954.
85. Puntoni F., Villa-Moruzzi E. Phosphorylation of the inhibitor-2 of protein phosphatase-1 by cdc2-cyclin B and GSK3. Biochem. Biophys. Res. Commun. 207:1995;732-739.
86. Fernandez A., Brautigan D.L., Lamb N.J.C. Protein phosphatase type 1 in mammalian cell mitosis: chromosomal localization and involvement in mitotic exit. J. Cell Biol. 116:1992;1421-1430.
87. Zhang J., Zhang L., Zhao S., Lee E.Y.C. Identification and characterization of human I-3. Biochemistry. 37:1998;16728-16734.