Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent

Cell

Volumn 89, Issue 6, 1997, Pages 875-886

  Ranganathan, Rama ^a,c   Lu, Kun Ping ^a,b   Hunter, Tony ^a   Noel, Joseph P ^a  

^a SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

^c HOWARD HUGHES MEDICAL INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLOPHILIN;

ARTICLE; CELL CYCLE; CRYSTAL STRUCTURE; ENZYME ANALYSIS; ENZYME PHOSPHORYLATION; ENZYME PURIFICATION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBUNIT; EUKARYOTE; HUMAN; MITOSIS; PRIORITY JOURNAL; X RAY CRYSTALLOGRAPHY;

EUKARYOTA;

EID: 0008233581     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80273-1     Document Type: Article

References (50)

1. Albers, M.W., Walsh, CT., and Schreiber, S.L. (1990). Substrate specificity for the human rotamase FKBP: a view of FK506 and rapamycin as leucine-(twisted amide)-proline mimics. J. Org. Chem. 55, 4984-4986.
2. Bacon, D., and Anderson, W.F. (1988). A fast algorithm for rendering space-filling molecule pictures. J. Mol. Graphics 6, 219-220.
3. Baker, E.K., Colley, N.J., and Zuker, C.S. (1994). The cyclophilin homolog ninaA functions as a chaperone, forming a stable complex in vivo with its protein target rhodopsin. EMBO J. 13, 4886-4895.
4. Brunger, A.T. (1992). X-PLOR Version 3.1: A System for X-Ray Crystallography and NMR (New Haven, Connecticut: Department of Molecular Biophysics and Biochemistry and Howard Hughes Medical Institute, Yale University).
5. Carson, M., and Bugg, C.E. (1986). Algorithm for ribbon models of proteins. J. Mol. Graphics 4, 121-122.
6. Chan, D.C., Bedford, M.T., and Leder, P. (1996). Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains. EMBO J. 15, 1045-1054.
7. Clackson, T., and Wells, J.A. (1995). A hot spot of binding energy in a hormone-receptor interface. Science 267, 383-386.
8. Colley, N.J., Baker, E.K., Stamnes, M .A., and Zuker, C.S. (1991). The cyclophilin homolog ninaA is required in the secretory pathway. Cell 67, 255-263.
9. Cowtan, K.D. (1994). 'dm': an automated procedure for phase improvement by density modification. Joint CCP4 and ESF-EACBM Newsletter on Protein Crystallography 31, pp. 34-38.
10. Creighton,T.E. (1993). Proteins Structures and Molecular Properties (New York: W.H. Freeman and Company).
11. Ferrin, T.E., Huang, C.C., Jarvis, L.E., and Langridge, R. (1988). The MIDAS display system. J. Mol. Graphics 6, 13-27.
12. Fischer, G., Wittmann-Liebold, B., Lang, K., Kiefhaber, T., and Schmid, F.X. (1989). Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins. Nature 337, 476-478.
13. Fischer, S., Michnick, S., and Karplus, M. (1993). A mechanism for rotamase catalysis by the FK506 binding protein (FKBP). Biochemistry 32, 13830-13837.
14. Gamble, T.R., Vajdos, F.F., Yoo, S., Worthylake, D.K., Houseweart, M., Sundquist, W.I., and Hill, C.P. (1996). Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid. Cell 87, 1285-1294.
15. Hanes, S.D., Shank, P.R., and Bostian, K.A. (1989). Sequence and mutational analysis of ESS1, a gene essential for growth in Saccharomyces cerevisiae. Yeast 5, 55-72.
16. Harrison, R.K., and Stein, R.L. (1990a). Mechanistic studies of peptidyl prolyl cis-trans isomerase: evidence for catalysis by distortion. Biochemistry 29, 1684-1689.
17. Harrison, R.K., and Stein, R.L. (1990b). Substrate specificities of the peptidyl prolyl cis-trans isomerase activities of cyclophilin and FK-506 binding protein: evidence for the existence of a family of distinct enzymes. Biochemistry 29, 3813-3816.
18. Heitman, J., Koller, A., Cardena, M.E., and Hall, M.N. (1993). Identification of immunosuppressive drug targets in yeast. METHODS: A Companion to Methods in Enzymology 5, 176-187.
19. Hemenway, C.S., and Heitman, J. (1996). Immunosuppressent target protein FKBP12 is required for P-glycoprotein function in yeast. J. Biol. Chem. 271, 18527-18534.
20. Huang, C.C., Petersen, E.F., Klein, T.E., Ferrin, I.E., and Langridge, R. (1991). Conic: a fast renderer for space-filling molecules with shadows. J. Mol. Graphics 9, 230-236.
21. Janin, J., and Chothia, C. (1990). The structure of protein-protein recognition sites. J. Biol. Chem. 265, 16027-16030.
22. Jones, T.A., Zou, J.Y., Cowan, S., and Kjeldgaard, M. (1991). Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A47, 110-119.
23. King, R.W., Jackson, P.K., and Kirschner, M.W. (1994). Mitosis in transition. Cell 79, 563-571.
24. Kofron, J.L., Kuzmic, P., Kishore, V., Colon-Bonilla, E., and Rich, D.H. (1991). Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay. Biochemistry 30, 6127-6134.
25. Kraulis, P. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
26. Lu, K.P., and Hunter, T. (1995). Evidence for a NIMA-like mitotic pathway in vertebrate cells. Cell 81, 413-424.
27. Lu, K.P., and Means, A.R. (1994). Expression of the noncatalytic domain of the NIMA kinase causes a G2 arrest in Aspergillus nidulans. EMBO J. 13, 2103-2113.
28. Lu, K.P., Osmani, S.A., and Means, A.R. (1993). Properties and regulation of the cell cycle-specific NIMA protein kinase of Aspergillus nidulans. J. Biol. Chem. 268, 8769-8776.
29. Lu, K.P., Hanes, S.D., and Hunter, T. (1996). A human peptidyl-prolyl isomerase essential for regulation of mitosis. Nature 380, 544-547.
30. Macias, M.J., Hyvonen, M., Baraldi, E., Schultz, J., Sudol, M., Saraste, M., and Oschkinat, H. (1996). Structure of the WW domain of a kinase-associated protein complexed with a proline-rich peptide. Nature 382, 646-649.
31. Matouschek, A., Rospert, S., Schmid, K., Glick, B.S., and Schatz, G. (1995). Cyclophilin catalyzes protein folding in yeast mitochondria. Proc. Natl. Acad. Sci. USA 92, 6319-6323.
32. Miller, S., Janin, J., Lesk, A.M., and Chothia, C. (1987). Interior and surface of monomeric proteins. J. Mol. Biol. 196, 641-656.
33. Nicholls, A., Sharp, K.A., and Honig, B. (1991). Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11, 281-296.
34. Nurse, P. (1994). Ordering S phase and M phase in the cell cycle. Cell 79, 547-550.
35. Osmani, A.H. McGuire, S.L., and Osmani, S.A. (1991) Parallel activation of the NIMA and p34cdc2 cell cycle-regulated protein kinases is required to initiate mitosis in A. nidulans. Cell 67, 283-291.
36. Otwinowski, Z. (1991). ML-PHARE (Warrington, England: Science and Engineering Research Council Collaborative Computing Project Number 4, Daresbury Laboratory).
37. Otwinowski, Z. (1993). Oscillation data reduction program. In Data Collection and Processing, L. Sawyer, N. Issacs, and S. Bailey, eds. (Warrington, England: Science and Engineering Research Council, Daresbury Laboratory), pp. 55-62.
38. Park, ST., Aldape, R.A., Futer, O., DeCenzo, M.T., and Livingston, D.J. (1992). PPlase catalysis by human FK506-binding protein proceeds through a conformational twist mechanism. J. Biol. Chem. 267, 3316-3324.
39. Rassow, J., Mohrs, K., Koidl, S., Barthelmess, I.B., Pfanner, N., and Tropschug, M. (1995). Cyclophilin 20 is involved in mitochondrial protein folding in cooperation with molecular chaperones Hsp70 and Hsp60. Mol. Cell. Biol. 15, 2654-2662.
40. Schmid, F.X. (1995). Prolyl isomerases join the fold. Curr. Biol. 5, 993-994.
41. Schreiber, S.L., and Crabtree, G.R. (1992). The mechanism of action of cyclosporin A and FK506. Immunol. Today 13, 136-142.
42. Staub, O., and Rotin, D. (1996). WW domains. Structure 4, 495-499.
43. Stein, R.L.(1993). Mechanism of enzymatic and nonenzymatic prolyl cis-trans isomerization. Adv. Prot. Chem. 44, 1-24.
44. Steinmann, B., Bruckner, P., and Supertifurga, A. (1991). Cyclosporin-A slows collagen triple-helix formation in vivo - indirect evidence for a physiologic role of peptidyl-prolyl cis-frans-isomerase. J. Biol. Chem. 266, 1299-1303.
45. Sudol, M. (1996a). Structure and function of the WW Domain. Prog. Biophys. Mol. Biol. 65, 113-132.
46. Sudol, M. (1996b). The WW module competes with the SH3 domain? Trends Biochem. Sci. 21, 161-163.
47. Sudol, M., Chen,H.I., Bougeret, C., Einbond, A., and Bork, P. (1995). Characterization of a novel protein-binding module - the WW domain. FEBS Lett. 369, 67-71.
48. Van Duyne, G.D., Standaert, R.F., Karplus, P.A., Schreiber, S.L., and Clardy, J. (1993). Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and Rapamycin. J. Mol. Biol. 229, 105-124.
49. Ye, X.S., Xu, G., Pu, R.T., Fincher, R.R., McGuire, S.L., Osmani, A.H., and Osmani,S.A. (1995).The NIMA protein kinase hyperphosphorylated and activated downstream of p34cdc2/cyclin B: coordination of two mitosis promoting kinases. EMBO J. 14, 986-994.
50. Young, L., Jernigan, R.L., and Covell, D.G. (1994). A role for surface hydrophobicity in protein-protein recognition. Prot. Sci. 3,717-729.