Role of Intrinsic Flexibility in Signal Transduction Mediated by the Cell Cycle Regulator, p27Kip1

Journal of Molecular Biology

Volumn 376, Issue 3, 2008, Pages 827-838

  Galea, Charles A ^a   Nourse, Amanda ^a   Wang, Yuefeng ^a   Sivakolundu, Sivashankar G ^a   Heller, William T ^b   Kriwacki, Richard W ^a,c  

^a ST JUDE CHILDREN S RESEARCH HOSPITAL   (United States)

^b OAK RIDGE NATIONAL LABORATORY   (United States)

^c UNIVERSITY OF TENNESSEE HEALTH SCIENCE CENTER   (United States)

Author keywords

cell cycle; cyclin dependent kinase inhibitor; disordered protein; intrinsically unstructured protein; p27Kip1

Indexed keywords

CYCLIN A; CYCLIN DEPENDENT KINASE; CYCLIN DEPENDENT KINASE INHIBITOR 1B;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CELL CYCLE REGULATION; CELL DIVISION; MOLECULAR DYNAMICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN MODIFICATION; PROTEIN PROCESSING; REGULATORY MECHANISM; SIGNAL TRANSDUCTION;

EUKARYOTA;

EID: 39049162291     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.12.016     Document Type: Article

References (50)

1. Hengst L., Dulic V., Slingerland J.M., Lees E., and Reed S.I. A cell cycle-regulated inhibitor of cyclin-dependent kinases. Proc. Natl Acad. Sci. USA 91 (1994) 5291-5295
2. Polyak K., Kato J.Y., Solomon M.J., Sherr C.J., Massague J., Roberts J.M., and Koff A. p27kip1, a cyclin-Cdk inhibitor, links transforming growth factor-beta and contact inhibition to cell cycle arrest. Genes Dev. 8 (1994) 9-22
3. Toyoshima H., and Hunter T. p27, a novel inhibitor of G1 cyclin-Cdk protein kinase activity, is related to p21. Cell 78 (1994) 67-74
4. Lacy E.R., Filippov I., Lewis W.S., Otieno S., Xiao L., Weiss S., et al. p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding. Nat. Struct. Mol. Biol. 11 (2004) 358-364
5. Morgan D.O. Principles of CDK regulation. Nature 374 (1995) 131-134
6. Hengst L., and Reed S.I. Inhibitors of the Cip/Kip family. Curr. Top. Microbiol. Immunol. 227 (1998) 25-41
7. Sherr C.J., and Roberts J.M. CDK inhibitors: positive and negative regulators of G1-phase progression. Genes Dev. 13 (1999) 1501-1512
8. Hengst L., and Reed S.I. Translational control of p27Kip1 accumulation during the cell cycle. Science 271 (1996) 1861-1864
9. Pagano M., Tam S.W., Theodoras A.M., Beer-Romero P., Del Sal G., Chau V., et al. Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27. Science 269 (1995) 682-685
10. Grimmler M., Wang Y., Mund T., Cilensek Z., Keidel E.M., Waddell M.B., et al. Cdk-inhibitory activity and stability of p27(Kip1) are directly regulated by oncogenic tyrosine kinases. Cell 128 (2007) 269-280
11. Bloom J., and Pagano M. Deregulated degradation of the cdk inhibitor p27 and malignant transformation. Semin. Cancer. Biol. 13 (2003) 41-47
12. Bloom J., Pagano M., Ababou M., Dutertre S., Lecluse Y., Onclercq R., et al. Deregulated degradation of the cdk inhibitor p27 and malignant transformation ATM-dependent phosphorylation and accumulation of endogenous BLM protein in response to ionizing radiation; a comparison of cell cycle markers in well-differentiated lobular and ductal carcinomas MNNG-transformed Bloom syndrome B-lymphoblastoids for the detection of Hodgkin's lymphoma-associated antigen in 2D Westerns. Semin. Cancer. Biol. 13 (2003) 41-47
13. Slingerland J., and Pagano M. Regulation of the cdk inhibitor p27 and its deregulation in cancer. J. Cell Physiol. 183 (2000) 10-17
14. Kamura T., Hara T., Matsumoto M., Ishida N., Okumura F., Hatakeyama S., et al. Cytoplasmic ubiquitin ligase KPC regulates proteolysis of p27(Kip1) at G1 phase. Nat. Cell Biol. 6 (2004) 1229-1235
15. Kotoshiba S., Kamura T., Hara T., Ishida N., and Nakayama K.I. Molecular dissection of the interaction between p27 and Kip1 ubiquitylation-promoting complex, the ubiquitin ligase that regulates proteolysis of p27 in G1 phase. J. Biol. Chem. 280 (2005) 17694-17700
16. Sabile A., Meyer A.M., Wirbelauer C., Hess D., Kogel U., Scheffner M., and Krek W. Regulation of p27 degradation and S-phase progression by Ro52 RING finger protein. Mol. Cell Biol. 26 (2006) 5994-6004
17. Chu I., Sun J., Arnaout A., Kahn H., Hanna W., Narod S., et al. p27 phosphorylation by Src regulates inhibition of cyclin E-Cdk2. Cell 128 (2007) 281-294
18. Russo A.A., Jeffrey P.D., Patten A.K., Massague J., and Pavletich N.P. Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex. Nature 382 (1996) 325-331
19. Bienkiewicz E.A., Adkins J.N., and Lumb K.J. Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27(Kip1). Biochemistry 41 (2002) 752-759
20. Sivakolundu S.G., Bashford D., and Kriwacki R.W. Disordered p27(Kip1) exhibits intrinsic structure resembling the Cdk2/cyclin A-bound conformation. J. Mol. Biol. 353 (2005) 1118-1128 (Epub 2005 Sep 20)
21. Koradi, R., Billeter, M. & Wuthrich, K. (1996). MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics, 14, 51-55, 29-32.
22. Garcia de la Torre J. Building hydrodynamic bead-shell models for rigid bioparticles of arbitrary shape. Biophys. Chem. 94 (2001) 265-274
23. Garcia De La Torre J., Huertas M.L., and Carrasco B. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78 (2000) 719-730
24. Svergun D.I. Determination of the regularization parameter in indirect-transform methods using perceptual criteria. J. Appl. Crystallogr. 25 (1992) 495-503
25. Heller W.T., Krueger J.K., and Trewhella J. Further insights into calmodulin-myosin light chain kinase interaction from solution scattering and shape restoration. Biochemistry 42 (2003) 10579-10588
26. Kozin M.B., and Svergun D.I. Automated matching of high- and low-resolution structural models. J. Appl. Crystallogr. 34 (2001) 33-41
27. Guinier A., and Fournet G. Small-Angle Scattering of X-rays (1955), John Wiley & Sons, New York
28. Debye P. Molecular-weight determination by light scattering. J. Phys. Colloid Chem. 51 (1947) 18-32
29. Tjioe E., and Heller W.T. ORNL_SAS: software for calculation of small-angle scattering intensities of proteins and protein complexes. J. Appl. Crystallogr. 40 (2007) 782-785
30. Heller W.T. Influence of multiple well defined conformations on small-angle scattering of proteins in solution. Acta Crystallogr., Sect. D: Biol. Crystallogr. 61 (2005) 33-44
31. Bienkiewicz E.A., Adkins J.N., and Lumb K.J. Functional consequences of preorganized helical structure in the intrinsically disordered cell-cycle inhibitor p27(Kip1). Biochemistry 41 (2002) 752-759
32. Hao B., Zheng N., Schulman B.A., Wu G., Miller J.J., Pagano M., and Pavletich N.P. Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase. Mol. Cell 20 (2005) 9-19
33. Buck M., Xu W., and Rosen M.K. A two-state allosteric model for autoinhibition rationalizes WASP signal integration and targeting. J. Mol. Biol. 338 (2004) 271-285
34. Remenyi A., Good M.C., and Lim W.A. Docking interactions in protein kinase and phosphatase networks. Curr. Opin. Struct. Biol. 16 (2006) 676-685
35. Neduva V., and Russell R.B. Linear motifs: evolutionary interaction switches. FEBS Lett. 579 (2005) 3342-3345
36. Kriwacki R.W., Hengst L., Tennant L., Reed S.I., and Wright P.E. Structural studies of p21(waf1/cip1/sdi1) in the free and Cdk2-bound state: Conformational disorder mediates binding diversity. Proc. Natl Acad. Sci. USA 93 (1996) 11504-11509
37. Grimmler M., Wang Y., Mund T., Cilensek Z., Keidel E.M., Waddell M.B., et al. Cdk-inhibitory activity and stability of p27Kip1 are directly regulated by oncogenic tyrosine kinases. Cell 128 (2007) 269-280
38. Wang Y., Filippov I., Richter C., Luo R., and Kriwacki R.W. Solution NMR studies of an intrinsically unstructured protein within a dilute, 75 kDa eukaryotic protein assembly; probing the practical limits for efficiently assigning polypeptide backbone resonances. ChemBioChem 6 (2005) 2242-2246
39. Neidhardt F.C., Bloch P.L., and Smith D.F. Culture medium for enterobacteria. J. Bacteriol. 119 (1974) 736-747
40. Grzesiek S., and Bax A. Improved 3D triple resonance NMR techniques applied to a 31 kDa protein. J. Magn. Reson. 96 (1992) 432-440
41. Grzesiek S., Dobeli H., Gentz R., Garotta G., Labhardt A.M., and Bax A. 1H, 13C, and 15N NMR backbone assignments and secondary structure of human interferon-gamma. Biochemistry 31 (1992) 8180-8190
42. Wittekind M., and Mueller L. HNCACB, a high-sensitivity 3D NMR experiment to correlate amide-proton and nitrogen resonances with the alpha- and beta-carbon resonances in proteins. J. Magn. Reson. B 101 (1993) 201-205
43. Yamazaki T., Lee W., Arrowsmith C.H., Muhandiram D.R., and Kay L.E. A suite of triple resonance NMR experiments for the backbone assignment of 15N, 13C, 2H labeled proteins with high sensitivity. J. Am. Chem. Soc. 116 (1994) 11655-11666
44. Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., and Bax A. NMR Pipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6 (1995) 277-293
45. Cavanagh J., Fairbrother III W.J., Palmer A.G., and Skelton N.J. Protein NMR Spectroscopy (1996), Academic Press, New York
46. Schwarzinger S., Kroon G.J., Foss T.R., Chung J., Wright P.E., and Dyson H.J. Sequence-dependent correction of random coil NMR chemical shifts. J. Am. Chem. Soc. 123 (2001) 2970-2978
47. Vistica J., Dam J., Balbo A., Yikilmaz E., Mariuzza R.A., Rouault T.A., and Schuck P. Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition. Anal. Biochem. 326 (2004) 234-256
48. Case D.A., Darden T.A., Cheatham I.T.E., Simmerling C.L., Wang J., Duke R.E., et al. AMBER 9 (2006), University of California, San Francisco
49. Woodward J.D., Pickel J.M., Anovitz L.M., Heller W.T., and Rondinone A.J. Self-assembled colloidal crystals from ZrO2 nanoparticles. J. Phys. Chem. B 110 (2006) 19456-19460
50. Taylor J.R. An Introduction to Error Analysis: The Study of Uncertainties in Physical Measurements. 2nd edit. (1997), University Science Books, Sausalito, CA