Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: A model for activator:coactivator interactions

Cell

Volumn 91, Issue 6, 1997, Pages 741-752

  Radhakrishnan, Ishwar ^a   Pérez Alvarado, Gabriela C ^a   Parker, David ^b   Dyson, H Jane ^a   Montminy, Marc R ^b   Wright, Peter E ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; NUCLEAR FACTOR;

ARTICLE; CELL INTERACTION; COMPLEX FORMATION; DNA HELIX; ENZYME INDUCTION; ENZYME PHOSPHORYLATION; GENE EXPRESSION REGULATION; GENE TARGETING; HORMONAL REGULATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; TARGET CELL; TRANSACTIVATION;

EID: 0344936739     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(00)80463-8     Document Type: Article

References (56)

1. Akimaru, H., Chen, Y., Dai, P., Hou, D.-X., Nonaka, M., Smolik, S.M., Armstrong, S., Goodman, R.H., and Ishii, S. (1997). Drosophila CBP is a co-activator of cubitus interruptus in hedgehog signaling. Nature 386, 735-738.
2. Altschul, S.F., Gish, W., Miller, W., Myers, E.W., and Lipman, D.J. (1990). Basic local alignment search tool. J. Mol. Biol. 215, 403-410.
3. Arias, J., Alberts, A.S., Bindle, P., Claret, F.X., Smeal, T., Karin, M., Feramisco, J., and Montminy, M. (1994). Activation of cAMP and mitogen responsive genes relies on a common nuclear factor. Nature 370, 226-229.
4. Bannister, A.J., and Kouzarides, T. (1996). The CBP co-activator is a histone acetyltransferase. Nature 384, 641-643.
5. Bannister, A.J., Oehler, T., Wilhelm, D., Angel, P., and Kouzarides, T. (1995). Stimulation of c-Jun activity by CBP: c-Jun residues Ser63/ 73 are required for CBP induced stimulation in vivo and CBP binding in vitro. Oncogene 11, 2509-2514.
6. Bax, A., and Grzesiek, S. (1993). Methodological advances in protein NMR. Acc. Chem. Res 26, 131-138.
7. Bhattacharya, S., Eckner, R., Grossman, S., Oldread, E., Arany, Z., D'Andrea, A., and Livingston, D.M. (1996). Cooperation of Stat2 and p300/CBP in signaling induced by interferon-α. Nature 383, 344-347.
8. Brindle, P., Linke, S., and Montminy, M. (1993). Analysis of a PK-A dependent activator in CREB reveals a new role for the CREM family of repressers. Nature 364, 821-824.
9. Brinkmann, U., Mattes, R.E., and Buckel, P. (1989). High-level expression of recombinant genes in Escherichia coli is dependent on the availability of the dnaY gene product. Gene 85, 109-114.
10. Chakravarti, D., LaMorte, V.J., Nelson, M.C., Nakajima, T., Schulman, I.G., Juguilon, H., Montminy, M., and Evans, R.M. (1996). Role of CBP/P300 in nuclear receptor signaling. Nature 383, 99-103.
11. Chrivia, J.C., Kwok, R.P., Lamb, N., Hagiwara, M., Montminy, M., and Goodman, R.H. (1993). Phosphorylated CREB binds specifically to nuclear protein CBP. Nature 365, 855-859.
12. Clore, G.M., and Gronenborn, A.M. (1994). Multidimensional heteronuclear Nuclear Magnetic Resonance of proteins. Meth. Enzymol 239, 349-363.
13. Copley, R.R., and Barton, G.J. (1994). A structural analysis of phosphate and sulphate binding sites in proteins: estimation of propensities for binding and conservation of phosphate binding sites. J. Mol. Biol. 242, 321-329.
14. Dai, P., Akimaru, H., Tanaka, Y., Hou, D.X., Yasukawa, T., KaneiIshii, C., Takahashi, T., and Ishii, S. (1996). CBP as a transcriptional coactivator of c-Myb. Genes Dev. 10, 528-540.
15. Ferreri, K., Gill, G., and Montminy, M. (1994). The cAMP regulated transcription factor CREB interacts with a component of the TFIID complex. Proc. Natl. Acad. Sci. USA. 91, 1210-1213.
16. Flocco, M.M., and Mowbray, S.L. (1994). Planar stacking interactions of arginine and aromatic side-chains in proteins. J. Mol. Biol. 235, 709-717.
17. Gonzalez, G.A., and Montminy, M.R. (1989). Cyclic AMP stimulates somatostatin gene transcription by phosphorylation of CREB at serine-133. Cell 59, 675-680.
18. Gonzalez, G.A., Yamamoto, K.K., Fischer, W.H., Karr, D., Menzel, P., Biggs, W., III, Vale, W.W., and Montminy, M.R. (1989). A cluster of phosphorylation sites on the cyclic AMP-regulated nuclear factor CREB predicted by its sequence. Nature 337, 749-752.
19. Gonzalez, G.A., Menzel, P., Leonard, J., Fischer, W.H., and Montminy, M. (1991). Characterization of motifs which are critical for activity of the cyclic AMP-responsive transcription factor CREB. Mol. Cell. Biol. 11, 1306-1312.
20. Güntert, P., and Wüthrich, K. (1991). Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints. J. Biomol. NMR 1, 447-456.
21. Güntert, P., Braun, W., and Wüthrich, K. (1991). Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J. Mol. Biol. 217, 517-530.
22. Hagiwara, M., Alberts, A., Brindle, P., Meinkoth, J., Feramisco, J., Deng, T., Karin, M., Shenolikar, S., and Montminy, M. (1992). Transcriptional attenuation following cAMP induction requires PP-1-mediated dephosphorylation of CREB. Cell 70, 105-113.
23. Holm, L., and Sander, C. (1994). The FSSP database of structurally aligned protein fold families. Nucl. Acids Res. 22, 3600-3609.
24. Hutchinson, E.G., and Thornton, J.M. (1996). PROMOTIF-A program to identify and analyze structural motifs in proteins. Protein Sci. 5, 212-220.
25. Janknecht, R., and Hunter, T. (1996). Transcriptional control: versatile molecular glue. Curr. Biol. 6, 951-954.
26. Janknecht, R., and Nordheim, A. (1994). Regulation of the c-fos promoter by the ternary complex factor Sap-1 a and its coactivator CBP. Oncogene 12, 1961-1969.
27. Kamei, Y., Xu, L., Heinzel, T., Torchia, J., Kurokawa, R., Gloss, B., Lin, S.-C., Heyman, R.A., Rose, D.W., Glass, C.K., and Rosenfeld, M.G. (1996). ACBP integrator complex mediates transcriptional activation and AP-1 inhibition by nuclear receptors. Cell 85, 403-414.
28. Kee, B., Arias, J., and Montminy, M. (1996). Adaptor mediated recruitment of RNA polymerase II to a signal dependent activator. J. Biol. Chem. 271, 2373-2375.
29. Knighton, D.R., Zheng, J., Eyck, L.F.T., Ashford, V.A., Xuong, N.-H., Taylor, S.S., and Sowadski, J.M. (1991 a). Crystal structure of the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 407-420.
30. Knighton, D.R., Zheng, J., Ten Eyck, L.F., Xuong, N.-H., Taylor, S.S., and Sowadski, J.M. (1991b). Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase. Science 253, 414-420.
31. N-Hα J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods. J. Biomol. NMR 4, 871-878.
32. Kussie, P.H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A.J., and Pavletich, N.P. (1996). Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain. Science 274, 948-953.
33. Kwok, R.P.S., Lundblad, J.R., Chrivia, J.C., Richards, J.P., Bächinger, H.P., Brennan, R.G., Roberts, S.G.E., Green, M.R., and Goodman, R.H. (1994). Nuclear protein CBP is a coactivator for the transcription factor CREB. Nature 370, 223-226.
34. Kwok, R.P.S., Laurance, M.E., Lundblad, J.R., Goldman, P.S., Shih, H., Connor, L.M., Marriott, S.J., and Goodman, R.H. (1996). Control of cAMP-regulated enhancers by the viral transactivator Tax through CREB and the co-activator CBP. Nature 380, 642-646.
35. Laskowski, R.A., Rullmann, J.A.C., MacArthur, M.W., Kaptein, R., and Thornton, J.M. (1996). AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8, 477-486.
36. 13C HMQC-NOESY experiment for extracting intermolecular NOE contacts in molecular complexes. FEBS Lett. 350, 87-90.
37. 13C-labeled proteins. J. Magn. Reson. Series B 112, 259-268.
38. Mayer, B.J., Jackson, P.K., Van Etten, R.A., and Baltimore, D. (1992). Point mutationsin the ab/SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo. Mol. Cell. Biol. 12, 609-618.
39. Mitchell, J.B.O., Nandi, C.L., McDonald, I.K., Thornton, J.M., and Price, S.L. (1994). Amino/aromatic interactions in proteins: is the evidence stacked against hydrogen bonding? J. Mol. Biol. 239, 315-331.
40. Nakajima, T., Uchida, C., Anderson, S., Parvin, J., and Montminy, M. (1997a). RNA helicase A mediates association of CBP with RNA polymerase II. Cell 90, 1107-1112.
41. Nakajima, T., Uchida, C., Anderson, S., Parvin, J., and Montminy, M. (1997b). Analysis of a cAMP responsive activator reveals a two-component mechanism for transcriptional induction via signal-dependent factors. Genes Dev. 11, 738-747.
42. 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.
43. Ogryzko, V.V., Schiltz, R.L., Russanova, V., Howard, B.H., and Nakatani, Y. (1996). The transcriptional coactivators p300 and CBP are histone acetyltransferases. Cell 87, 953-959.
44. 1H]-NMR spectroscopy: combined use with isotope labelling for studies of macromolecular conformation and intermolecular interactions. Quart. Rev. Biophys. 23, 39-96.
45. Parker, D., Ferreri, K., Nakajima, T., LaMorte, V.J., Evans, R., Koerber, S.C., Hoeger, C., and Montminy, M. (1996). Phosphorylation of CREB at Ser 133 induces complex formation with CPB via a direct mechanism. Mol. Cell. Biol. 16, 694-703.
46. Pearlman, D.A., Case, D.A., Caldwell, J.W., Ross, W.S., Cheatham, T.E., III, Ferguson, D.M., Seibel, G.L., Singh, U.C., Weiner, P.K., and Kollman, P.A. (1995). AMBER 4.1. (San Francisco: University of California).
47. Ptashne, M., and Gann, A. (1997). Transcriptional activation by recruitment. Nature 386, 569-577.
48. Sanner, M.F., Olson, A.J., and Sphener, J.-C. (1996). Reduced surface: an efficient way to compute molecular surfaces. Biopolymers 38, 305-320.
49. Shih, H.M., Goldman, P.S., DeMaggio, A.J., Hollenberg, S.M., Goodman, R.H., and Hoekstra, M.F. (1996). A positive genetic selection for disrupting protein-protein interactions: identification of CREB mutations that prevent association with the coactivator CBP. Proc. Natl. Acad. Sci. USA. 93, 13896-13901.
50. 3C nuclear magnetic resonance chemical shifts. J. Am. Chem. Soc. 113., 5490-5492.
51. Uesugi, M., Nyanguile, O., Lu, H., Levine, A.J., and Verdine, G.L. (1997). Induced a helix in the VP16 activation domain upon binding to a human TAF. Science. 277, 1310-1313.
52. Upson, C., Faulhaber, T., Jr., Kamins, D., Laidlaw, D., Vroom, J., Gurwitz, R., and van Dam, A. (1989). The application visualization system: a computational environment for scientific visualization. IEEE Comp. Graph. Appl. 9, 30-42.
53. 13C. J. Am. Chem. Soc. 115, 5334-5335.
54. Waksman, G., Kominos, D., Robertson, S.C., Pant, N., Baltimore, D., Birge, R.B., Cowburn, D., Hanafusa, H., Mayer, B.J., Overduin, M., Resh, M.D., Rios, C.B., Silverman, L., and Kuriyan, J. (1992). Crystal structure of the phosphotyrosine recognition domain SH2 of v-src complexed with tyrosine-phosphorylated peptides. Nature. 358, 646-653.
55. 13C-labeled proteins via scalar couplings. J. Am. Chem. Soc. 115, 11054-11055.
56. Zhou, M.-M., Ravichandran, K.S., Olejniczak, ET., Petros, A.M., Meadows, R.P., Sattler, M., Harlan, J.E., Wade, W.S., Burakoff, S.J., and Fesik, S.W. (1995). Structure and ligand recognition of the phosphotyrosine binding domain of Shc. Nature 378, 584-592.