The nuclear receptor coactivator PGC-1α exhibits modes of interaction with the estrogen receptor distinct from those of SRC-1

Journal of Molecular Biology

Volumn 347, Issue 5, 2005, Pages 921-934

  Bourdoncle, Anne ^a   Labesse, Gilles ^a   Margueron, Raphaël ^b   Castet, Audrey ^b   Cavaillès, Vincent ^b   Royer, Catherine A ^a  

^a CENTRE DE BIOCHIMIE STRUCTURALE   (France)

^b INSERM   (France)

Author keywords

Anisotropy; Estrogen receptor; FCS; PGC 1; SRC 1

Indexed keywords

CELL NUCLEUS RECEPTOR; ESTROGEN RECEPTOR; ESTROGEN RECEPTOR ALPHA; ESTROGEN RECEPTOR BETA; FLUORESCENT DYE; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; STEROID RECEPTOR COACTIVATOR 1;

AMINO TERMINAL SEQUENCE; ANISOTROPY; ARTICLE; CARBOXY TERMINAL SEQUENCE; DNA BINDING; LIGAND BINDING; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN MOTIF; PROTEIN STRUCTURE; RNA BINDING; STOICHIOMETRY;

EID: 15244348980     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.01.048     Document Type: Article

References (54)

1. J. Xu, and Q. Li Review of the in vivo functions of the p160 steroid receptor coactivator family Mol. Endocrinol. 17 2003 1681 1692
2. P. Puigserver, Z. Wu, C.W. Park, R. Graves, M. Wright, and B.M. Spiegelman A cold-inducible coactivator of nuclear receptors linked to adaptive thermogenesis Cell 92 1998 829 839
3. P. Puigserver, and B.M. Spiegelman Peroxisome proliferator-activated receptor-gamma coactivator 1 alpha (PGC-1 alpha): transcriptional coactivator and metabolic regulator Endocr. Rev. 24 2003 78 90
4. D. Knutti, and A. Kralli PGC-1, a versatile coactivator Trends Endocrinol. Metab. 12 2001 360 365
5. D. Knutti, A. Kaul, and A. Kralli A tissue-specific coactivator of steroid receptors, identified in a functional genetic screen Mol. Cell. Biol. 20 2000 2411 2422
6. Z. Wu, P. Puigserver, U. Andersson, C. Zhang, G. Adelmant, and V. Mootha Mechanisms controlling mitochondrial biogenesis and respiration through the thermogenic coactivator PGC-1 Cell 98 1999 115 124
7. J.C. Yoon, P. Puigserver, G. Chen, J. Donovan, Z. Wu, and J. Rhee Control of hepatic gluconeogenesis through the transcriptional coactivator PGC-1 Nature 413 2001 131 138
8. I. Tcherepanova, P. Puigserver, J.D. Norris, B.M. Spiegelman, and D.P. McDonnell Modulation of estrogen receptor-alpha transcriptional activity by the coactivator PGC-1 J. Biol. Chem. 275 2000 16302 16308
9. R.B. Vega, J.M. Huss, and D.P. Kelly The coactivator PGC-1 cooperates with peroxisome proliferator-activated receptor alpha in transcriptional control of nuclear genes encoding mitochondrial fatty acid oxidation enzymes Mol. Cell. Biol. 20 2000 1868 1876
10. P. Delerive, Y. Wu, T.P. Burris, W.W. Chin, and C.S. Suen PGC-1 functions as a transcriptional coactivator for the retinoid X receptors J. Biol. Chem. 277 2002 3913 3917
11. S.N. Schreiber, D. Knutti, K. Brogli, T. Uhlmann, and A. Kralli The transcriptional coactivator PGC-1 regulates the expression and activity of the orphan nuclear receptor estrogen-related receptor alpha (ERRalpha) J. Biol. Chem. 278 2003 9013 9018
12. J. Lin, P. Puigserver, J. Donovan, P. Tarr, and B.M. Spiegelman Peroxisome proliferator-activated receptor gamma coactivator 1beta (PGC-1beta), a novel PGC-1-related transcription coactivator associated with host cell factor J. Biol. Chem. 277 2002 1645 1648
13. U. Andersson, and R.C. Scarpulla PGC-1-related coactivator, a novel, serum-inducible coactivator of nuclear respiratory factor 1-dependent transcription in mammalian cells Mol. Cell. Biol. 21 2001 3738 3749
14. D. Kressler, S.N. Schreiber, D. Knutti, and A. Kralli The PGC-1-related protein PERC is a selective coactivator of estrogen receptor alpha J. Biol. Chem. 277 2002 13918 13925
15. D. Knutti, D. Kressler, and A. Kralli Regulation of the transcriptional coactivator PGC-1 via MAPK-sensitive interaction with a repressor Proc. Natl Acad. Sci. USA 98 2001 9713 9718
16. P. Puigserver, G. Adelmant, Z. Wu, M. Fan, J. Xu, B. O'Malley, and B.M. Spiegelman Activation of PPARgamma coactivator-1 through transcription factor docking Science 286 1999 1368 1371
17. H. Oberkofler, H. Esterbauer, V. Linnemayr, A.D. Strosberg, F. Krempler, and W. Patsch Peroxisome proliferator-activated receptor (PPAR) gamma coactivator-1 recruitment regulates PPAR subtype specificity J. Biol. Chem. 277 2002 16750 16757
18. M. Monsalve, Z. Wu, G. Adelmant, P. Puigserver, M. Fan, and B.M. Spiegelman Direct coupling of transcription and mRNA processing through the thermogenic coactivator PGC-1 Mol. Cell 6 2000 307 316
19. A. Mayeda, G.R. Screaton, S.D. Chandler, X.D. Fu, and A.R. Krainer Substrate specificities of SR proteins in constitutive splicing are determined by their RNA recognition motifs and composite pre-mRNA exonic elements Mol. Cell. Biol. 19 1999 1853 1863
20. E. Margeat, N. Poujol, A. Boulahtouf, Y. Chen, J.D. Muller, and E. Gratton The human estrogen receptor alpha dimer binds a single SRC-1 coactivator molecule with an affinity dictated by agonist structure J. Mol. Biol. 306 2001 433 442
21. E. Lacroix, A.R. Viguera, and L. Serrano Elucidating the folding problem of alpha-helices: local motifs, long-range electrostatics, ionic-strength dependence and prediction of NMR parameters J. Mol. Biol. 284 1998 173 191
22. E. Margeat, A. Bourdoncle, R. Margueron, N. Poujol, V. Cavailles, and C. Royer Ligands differentially modulate the protein interactions of the human estrogen receptors alpha and beta J. Mol. Biol. 326 2003 77 92
23. J. Liu, K.S. Knappenberger, H. Kack, G. Andersson, E. Nilsson, C. Dartsch, and C.W. Scott A homogeneous in vitro functional assay for estrogen receptors: coactivator recruitment Mol. Endocrinol. 17 2003 346 355
24. G. Lazennec, T.R. Ediger, L.N. Petz, A.M. Nardulli, and B.S. Katzenellenbogen Mechanistic aspects of estrogen receptor activation probed with constitutively active estrogen receptors: correlations with DNA and coregulator interactions and receptor conformational changes Mol. Endocrinol. 11 1997 1375 1386
25. D.M. Heery, E. Kalkhoven, S. Hoare, and M.G. Parker A signature motif in transcriptional co-activators mediates binding to nuclear receptors Nature 387 1997 733 736
26. T.A. Pham, Y.P. Hwung, D. Santiso-Mere, D.P. McDonnell, and B.W. O'Malley Ligand-dependent and -independent function of the transactivation regions of the human estrogen receptor in yeast Mol. Endocrinol. 6 1992 1043 1050
27. L. Tora, A. Mullick, D. Metzger, M. Ponglikitmongkol, I. Park, and P. Chambon The cloned human oestrogen receptor contains a mutation which alters its hormone binding properties EMBO J. 8 1989 1981 1986
28. M.T. Tzukerman, A. Esty, D. Santiso-Mere, P. Danielian, M.G. Parker, and R.B. Stein Human estrogen receptor transactivational capacity is determined by both cellular and promoter context and mediated by two functionally distinct intramolecular regions Mol. Endocrinol. 8 1994 21 30
29. Y. Wu, W.W. Chin, Y. Wang, and T.P. Burris Ligand and coactivator identity determines the requirement of the charge clamp for coactivation of the peroxisome proliferator-activated receptor gamma J. Biol. Chem. 278 2003 8637 8644
30. A. Warnmark, E. Treuter, J.A. Gustafsson, R.E. Hubbard, A.M. Brzozowski, and A.C. Pike Interaction of transcriptional intermediary factor 2 nuclear receptor box peptides with the coactivator binding site of estrogen receptor alpha J. Biol. Chem. 277 2002 21862 21868
31. A.K. Shiau, D. Barstad, P.M. Loria, L. Cheng, P.J. Kushner, D.A. Agard, and G.L. Greene The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen Cell 95 1998 927 937
32. J.M. Wurtz, W. Bourguet, J.P. Renaud, V. Vivat, P. Chambon, D. Moras, and H. Gronemeyer A canonical structure for the ligand-binding domain of nuclear receptors Nature Struct. Biol. 3 1996 206
33. R.T. Nolte, G.B. Wisely, S. Westin, J.E. Cobb, M.H. Lambert, and R. Kurokawa Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma Nature 395 1998 137 143
34. A. Lupas, D.M. Van, and J. Stock Predicting coiled coils from protein sequences Science 252 1991 1162 1164
35. C.L. Day, and T. Alber Crystal structure of the amino-terminal coiled-coil domain of the APC tumor suppressor J. Mol. Biol. 301 2000 147 156
36. Y. Shamoo, N. bdul-Manan, and K.R. Williams Multiple RNA binding domains (RBDs) just don't add up Nucl. Acids Res. 23 1995 725 728
37. M. Boyer, N. Poujol, E. Margeat, and C.A. Royer Quantitative characterization of the interaction between purified human estrogen receptor alpha and DNA using fluorescence anisotropy Nucl. Acids Res. 28 2000 2494 2502
38. N. Poujol, E. Margeat, S. Baud, and C.A. Royer RAR antagonists diminish the level of DNA binding by the RAR/RXR heterodimer Biochemistry 42 2003 4918 4925
39. C.A. Royer Improvements in the numerical analysis of thermodynamic data from biomolecular complexes Anal. Biochem. 210 1993 91 97
40. C.A. Royer, and J.M. Beechem Numerical analysis of binding data: advantages, practical aspects, and implications Methods Enzymol. 210 1992 481 505
41. C.A. Royer, W.R. Smith, and J.M. Beechem Analysis of binding in macromolecular complexes: a generalized numerical approach Anal. Biochem. 191 1990 287 294
42. A. Philips, D. Chalbos, and H. Rochefort Estradiol increases and anti-estrogens antagonize the growth factor-induced activator protein-1 activity in MCF7 breast cancer cells without affecting c-fos and c-jun synthesis J. Biol. Chem. 268 1993 14103 14108
43. D. Douguet, and G. Labesse Easier threading through web-based comparisons and cross-validations Bioinformatics 17 2001 752 753
44. L.A. Kelley, R.M. MacCallum, and M.J. Sternberg Enhanced genome annotation using structural profiles in the program 3D-PSSM J. Mol. Biol. 299 2000 499 520
45. J. Shi, T.L. Blundell, and K. Mizuguchi FUGUE: sequence-structure homology recognition using environment-specific substitution tables and structure-dependent gap penalties J. Mol. Biol. 310 2001 243 257
46. L.J. McGuffin, K. Bryson, and D.T. Jones The PSIPRED protein structure prediction server Bioinformatics 16 2000 404 405
47. K. Karplus, C. Barrett, and R. Hughey Hidden Markov models for detecting remote protein homologies Bioinformatics 14 1998 846 856
48. J.A. Cuff, M.E. Clamp, A.S. Siddiqui, M. Finlay, and G.J. Barton JPred: a consensus secondary structure prediction server Bioinformatics 14 1998 892 893
49. G. Labesse, and J. Mornon Incremental threading optimization (TITO) to help alignment and modelling of remote homologues Bioinformatics 14 1998 206 211
50. A. Sali, and T.L. Blundell Comparative protein modelling by satisfaction of spatial restraints J. Mol. Biol. 234 1993 779 815
51. M.J. Sippl Recognition of errors in three-dimensional structures of proteins Proteins: Struct. Funct. Genet. 17 1993 355 362
52. D. Eisenberg, R. Luthy, and J.U. Bowie VERIFY3D: assessment of protein models with three-dimensional profiles Methods Enzymol. 277 1997 396 404
53. C. Colovos, and T.O. Yeates Verification of protein structures: patterns of nonbonded atomic interactions Protein Sci. 2 1993 1511 1519
54. R.L. Dunbrack Jr, and M. Karplus Backbone-dependent rotamer library for proteins. Application to side-chain prediction J. Mol. Biol. 230 1993 543 574