Structural basis for the recognition of regulatory subunits by the catalytic subunit of protein phosphatase 1

EMBO Journal

Volumn 16, Issue 8, 1997, Pages 1876-1887

  Egloff, Marie Pierre ^a   Johnson, Deborah F ^b   Moorhead, Greg ^b   Cohen, Patricia T W ^b   Cohen, Philip ^b   Barford, David ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF DUNDEE   (United Kingdom)

Author keywords

Protein phosphatase 1; Recognition motif; Recognition site; Regulatory subunits; X ray crystallography

Indexed keywords

PEPTIDE; PHOSPHOPROTEIN PHOSPHATASE 1;

AMINO ACID SEQUENCE; ARTICLE; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ENZYME SUBUNIT; MAMMAL; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; AMINO ACIDS; ANIMALS; CATALYSIS; CONSERVED SEQUENCE; CRYSTALLOGRAPHY, X-RAY; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUSCLE, SKELETAL; PEPTIDES; PHOSPHOPROTEIN PHOSPHATASE; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN CONFORMATION; RABBITS; SACCHAROMYCES CEREVISIAE; SEQUENCE ALIGNMENT; SERINE;

LEPIDOPTERA; MAMMALIA;

EID: 0030977268     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.8.1876     Document Type: Article

References (67)

1. Aitken, A. and Cohen, P. (1982) Isolation and characterisation of active fragments of protein phosphatase inhibitor-1 from rabbit skeletal muscle. FEBS Lett., 147, 54-58.
2. Aitken, A., Bilham, T. and Cohen, P. (1982) Complete primary structure of protein phosphatase 1 inhibitor 1 from rabbit skeletal muscle. Eur. J. Biochem., 126, 235-246.
3. Alessi, D.R., McDougall, L.K., Sola, M.M., Ikebe, M. and Cohen, P. (1992) The control of protein phosphatase-1 by targeting subunits. Eur. J. Biochem., 210, 1023-1035.
4. Alessi, D.R., Street, A.J., Cohen, P. and Cohen, P.T.W. (1993) Inhibitor-2 functions like a chaperone to fold three expressed isoforms of mammalian protein phophatase-1 into a conformation with the specificity and regulatory properties of the native enzyme. Eur. J. Biochem., 213, 1055-1066.
5. Barford, D. and Keller, J.C. (1994) Co-crystallization of the catalytic subunit of the serine/threonine specific protein phosphatase 1 from human in complex with microcystin LR. J. Mol. Biol., 235, 763-766.
6. Barton, G.J., Cohen, P.T.W. and Barford, D. (1994) Conservation analysis and structure prediction of the protein serine/threonine phosphatases. Eur. J. Biochem., 220, 225-237.
7. Brünger, A.T. (1992) X-PLOR: Version 3.1; A System for Protein Crystallography and NMR. Yale University Press, New Haven, CT.
8. Beullens, M., Van Eynde, A., Stalmans, W. and Bollen, M. (1992) The isolation of novel inhibitory polypeptides of protein phosphatase 1 from bovine thymus nuclei. J. Biol. Chem., 267, 16538-16544.
9. Beullens, M., Van Eynde, A., Bollen, M. and Stalmans, W. (1993) Inactivation of nuclear inhibitory polypeptides of protein phosphatase-1 (NIPP-1) by protein kinase A. J. Biol. Chem., 268, 13172-13177.
10. Beullens, M., Stalmans, W. and Bollen, M. (1996) Characterisation of a ribosomal inhibitory polypeptide of protein phosphatase-1 from rat liver. Eur. J. Biochem., 239, 183-189.
11. Cohen, P. (1989) The structure and regulation of protein phosphatases. Annu. Rev. Biochem., 58, 453-508.
12. Cohen, P. (1992) Signal integration at the level of protein kinases, protein phosphatases and their substrates. Trends Biochem. Sci., 17, 408-413.
13. Cohen, P., Alemany, S., Hemmings, B.A., Resink, T.J., Stralfors, P. and Tung, H.Y.L. (1988) Protein phosphatase 1 and protein phosphatase 2A from rabbit skeletal muscle. Methods Enzymol., 159, 390-408.
14. Desdouits, F. et al. (1995) Mechanism of inhibition of protein phosphatase 1 by DARPP-32: studies with recombinant DARPP-32 and synthetic peptides. Biochem. Biophys. Res. Commun., 206, 653-658.
15. Derrick, J.P. and Wigley, D.B. (1992) Crystal structure of a streptococcal protein G domain bound to an Fab fragment. Nature, 359, 752-754.
16. Dingwall, C. and Laskey, R.A. (1991) Nuclear targeting sequences - a consensus? Trends Biochem. Sci., 16, 478-481.
17. L-subunit of PP1. FEBS Lett., 375, 294-298.
18. Doherty, M.J., Young, P.R. and Cohen, P.T.W. (1996) Amino acid sequence of a novel protein phosphatase 1 binding protein (R5) which is related to the liver and muscle specific glycogen binding subunits of protein phosphatase 1. FEBS Lett., 399, 339-343.
19. Doyle, D.A., Lee, A., Lewis, J., Kim, E., Sheng, M. and MacKinnon, R. (1996) Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell, 85, 1067-1076.
20. Durfee, T., Becherer, K., Chen, P.-L., Yeh, S.-H., Yang, Y., Kilburn, A.E., Lee, W.-H. and Elledge, S.J. (1993) The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. Genes Dev., 7, 555-569.
21. Egloff, M.-P., Cohen, P.T.W., Reinemer, P. and Barford, D. (1995) Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate. J. Mol. Biol., 254, 942-959.
22. Endo, S., Zhou, X., Connor, J., Wang, B. and Shenolikar, S. (1996) Multiple structural elements define the specificity of recombinant human inhibitor-1 as a protein phosphatase-1 inhibitor. Biochemistry, 35, 5220-5228.
23. Faux, M.C. and Scott, J.D. (1996) More on target with protein phosphorylation: conferring specificity by location. Trends Biochem. Sci., 21, 312-315.
24. Francois, J.M., Thompson-Jaeger, S., Skroch, J., Zellenka, U., Spevak, W. and Tatchell, K. (1992) GAC1 may encode a regulatory subunit for protein phosphatase type 1 in Saccharoymes cerevisiae. EMBO J., 11, 87-96.
25. Frederick, D.L. and Tatchell, K. (1996) The REG2 gene of Saccharomyces cerevisiae encodes a type 1 protein phosphatase-binding protein that functions with Reg1p and the Snf1 protein kinase to regulate growth. Mol. Cell Biol., 16, 2922-2931.
26. Furey, W. and Swaminathan, S. (1990) PHASES: a program package for the processing and analysis of diffraction data from macromolecules. Am. Crystallogr. Assoc. Meeting Summary, 18, 73.
27. Goldberg, J., Huang, H., Kwon, Y., Greengard, P. Nairn, A.C. and Kuriyan, J. (1995) Three dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1. Nature, 376, 745-753.
28. Griffith, J.P. et al. (1995) X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex. Cell, 82, 507-522.
29. Helps, N., Barker, H., Elledge, S.J. and Cohen, P.T.W. (1995) Protein phosphatase 1 interacts with p53BP2, a protein which binds in the tumour supressor p53. FEBS Lett., 377, 295-300.
30. Hemmings, H.C., Jr. Nairn, A.C., Elliot, J.R. and Greengard, P. (1990) Synthetic peptide analogs of DARPP-32, an inhibitor of protein phosphatase-1. J. Biol. Chem., 265, 20369-20376.
31. Hirano, K., Ito, M. and Hartshorne, D.J. (1995) Interaction of the ribosomal protein, L5, with protein phosphatase type 1. J. Biol. Chem., 270, 19786-19790.
32. Hirano, K., Erdodi, F., Patton, J.G. and Hartshorne, D.J. (1996) Interaction of protein phosphatase type 1 with a splicing factor. FEBS Lett., 389, 191-194.
33. Hubbard, M.J. and Cohen, P. (1989) Regulation of protein phosphatase-1G from rabbit skeletal muscle; 2. Catalytic subunit translocation is a mechanism for reversible inhibition towards glycogen bound substrates. Eur. J. Biochem., 186, 711-716.
34. Hubbard, M.J. and Cohen, P. (1993) On target with a new mechanism for the regulation of protein phosphorylation. Trends Biochem. Sci., 18, 172-177.
35. Hunter, T. (1995) Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signalling. Cell, 80, 225-236.
36. Jagiello, I., Beullens, M., Stalmans, W. and Bollen, M. (1995) Subunit structure and regulation of protein phosphatase-1 in rat liver nuclei. J. Biol. Chem., 270, 17257-17263.
37. Johnson, D.K. Moorhead, G., Caudwell, F.B., Cohen, P. Chen, Y.-H., Chen, M.-X. and Cohen, P.T.W. (1996) Identification of protein phosphatase-1-binding domains on the glycogen and myofibrillar targeting subunits. Eur. J. Biochem., 239, 317-325.
38. 21 subunit and with myosin. Eur. J. Biochem., in press.
39. Kissinger, C.R. et al. (1995) Crystal structure of human calcineurin and the human FKBP12-FK506-calcineurin complex. Nature, 378, 641-644.
40. Knighton, D.R., Zheng, J., Ten Eyck, L.F., Xuong, N.-H., Taylor, S.S. and Sowadski, J.M. (1991) Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science, 253, 414-420.
41. Kraulis, P.J. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr., 24, 946-950.
42. Lee, B. and Richards, F.M. (1971) The interpretation of protein structures: estimation of static accessibilty. J. Mol. Biol., 55, 379-400.
43. Mermoud, J.E., Cohen, P and Lamond, A.I. (1992) Ser/Thr-specific protein phosphatases are required for both catalytic steps of pre-mRNA splicing. Nucleic Acid Res., 20, 5263-5269.
44. Moorhead, G., MacKintosh, W., Morrice, N., Gallagher, T. and MacKintosh, C. (1994) Purification of type 1 protein (serine/threonine) phosphatases by microcystin-Sepharose affinity chromatography. FEBS Lett., 356, 46-50.
45. Moorhead, G., MacKintosh, C., Morrice, N. and Cohen, P. (1995) Purification of the hepatic glycogen-associated form of protein phosphatase-1 by microcystin-Sepharose affinity chromatography. FEBS Lett., 362, 101-105.
46. Nassar, N., Horn, G., Herrman, C., Scherer, A., McCormick, F. and Wittinghofer, A. (1995) The 2.2 Å crystal structure of the ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue. Nature, 375, 554-560.
47. Naumovski, L. and Cleary, M.L. (1996) The p53-binding protein p53BP2 also interacts with Bcl2 and impedes cell cycle progression at G2/M. Mol. Cell. Biol., 16, 3884-3892.
48. Navaza, J. (1992) AMoRe: a new package for molecular replacement. In Dodson, E.J., Grower, S. and Wolf, W. (eds), Proceedings of the CCP4 Study Weekend. SERC, Daresbury Laboratory, Warrington, UK, pp. 87-91.
49. Nelson, K.K., Holmes, M. and Lemmon, S.K. (1996) SCD5, a suppressor of clathrin deficiency encodes a novel protein with a late secretory function in yeast. Mol. Biol. Cell, 7, 245-260.
50. Nicholls, A. and Honig, B. (1991) A rapid finite difference algorithm, utilising successive over relaxation to solve the Poisson-Boltzmann equation. J. Comput. Chem., 12, 435-445.
51. Otwinowski, Z. (1993) DENZO. In Sawyer, L., Isaacs, N. and Bailey, S. (eds). Data Collection and Processing. SERC Daresbury Laboratory, Warrington, UK, pp. 56-62.
52. Pelham, H.R. (1992) The Florey Lecture, 1992. The secretion of proteins by cells. Proc. R. Soc. Lond. Ser. B, B250, 1-10.
53. Roussel, A. and Cambillau, C. (1992) TURBO-FRODO. Biographics, LCCMB, Marseille, France.
54. Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex. Nature, 382, 325-331.
55. Schelling, D.L., Leader, D.P., Zammit, V.A. and Cohen, P. (1988) Distinct type-1 protein phosphatases are associated with hepatic glycogen and microsomes. Biochim. Biophys. Acta, 927, 221-231.
56. Shenolikar, S. (1994) Protein serine/threonine phosphatases - new avenues for cell regulation. Annu. Rev. Cell Biol., 10, 56-86.
57. Stark, M. (1996) Yeast protein serine/threonine phosphatases: multiple roles and diverse forms of regulation. Yeast, 12, 1647-1675.
58. Stralfors, P. Hiraga, A. and Cohen, P. (1985) The protein phosphatases involved in cellular regulation. Purification and characterisation of the slycogen-bound form of protein phosphatase 1 from skeletal muscle. Eur. J. Biochem., 149, 295-303.
59. GL) subunit of slycogen-associated protein phosphatase. J. Biol. Chem., 266, 15782-15789.
60. Tu, J. and Carlson, M. (1995) REG1 binds to protein phosphatase type 1 and regulates glucose repression in Saccharoymes cerevisiae. EMBO J., 14, 5939-5946.
61. Tu, J. Song, W. and Carlson, M. (1996) Protein phosphatase type 1 interacts with proteins required for meiosis and other cellular processes in Saccharomyces cerevisiae. Mol. Cell. Biol., 16, 4199-1206.
62. Van Eynde, A., Beullens, M., Stalmans, W. and Bollen, M. (1994) Full activation of a nuclear species of PP1 by phosphorylation with protein kinase A and casein kinase 2. Biochem. J., 297, 447-449.
63. Van Eynde, A., Wera, S., Beullens, M., Torrekens, S., Van Leuven, F., Stalmans, W. and Bollen, M. (1995) Molecular cloning of NIPP-1, a nuclear inhibitor of protein phosphatase-1, reveals homology with polypeptides involved in RNA processing. J. Biol. Chem., 270, 28068-28074.
64. Wera, S. and Hemmings, B.A. (1995) Serine/threonine protein phosphatases. Biochem. J., 311, 17-29.
65. Williams, K.R., Hemmings, H.C., LoPresti, M.B., Konigsberg, W.H. and Greengard, P. (1986) DARPP-32: primary structure and homology with protein phosphatase inhibitor-1. J. Biol. Chem., 261, 1890-1903.
66. Zhou, M.M. et al. (1995) Structure and ligand recognition of the phosphotyrosine binding domain of SHC. Nature, 378, 584-592.
67. Zhu, L., Harlow, E. and Dynlacht, B.D. (1995) p107 uses a p21CIP1-related domain to bind to cyclin/cdk2 and regulate interactions with E2F. Genes Dev., 9, 1740-1752.