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Science 12 June 1998:
Vol. 280. no. 5370, pp. 1747 - 1749
DOI: 10.1126/science.280.5370.1747
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Reports

Hormone-Dependent Coactivator Binding to a Hydrophobic Cleft on Nuclear Receptors

Weijun Feng, Ralff C. J. Ribeiro, Richard L. Wagner, Hoa Nguyen, James W. Apriletti, Robert J. Fletterick, John D. Baxter, Peter J. Kushner, * Brian L. West *

The ligand-binding domain of nuclear receptors contains a transcriptional activation function (AF-2) that mediates hormone-dependent binding of coactivator proteins. Scanning surface mutagenesis on the human thyroid hormone receptor was performed to define the site that binds the coactivators, glucocorticoid receptor-interacting protein 1 (GRIP1) and steroid receptor coactivator 1 (SRC-1). The residues involved encircle a small surface that contains a hydrophobic cleft. Ligand activation of transcription involves formation of this surface by folding the carboxyl-terminal alpha  helix against a scaffold of three other helices. These features may represent general ones for nuclear receptors.

W. Feng, H. Nguyen, J. W. Apriletti, J. D. Baxter, P. J. Kushner, B. L. West, Metabolic Research Unit, Box 0540, University of California San Francisco, San Francisco, CA 94143-0540, USA.
R. C. J. Ribeiro, Department of Pharmaceutical Sciences, University of Brasilia, D.F., Brazil.
R. L. Wagner and R. J. Fletterick, Department of Biochemistry and Biophysics, S1058, University of California San Francisco, San Francisco, CA 94143, USA.
*   To whom correspondence should be addressed. E-mail: west{at}socrates.ucsf.edu (B.L.W.) or kushner{at}itsa.ucsf.edu (P.J.K.)

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J. Biol. Chem. 278, 6912-6920
   Abstract »    Full Text »    PDF »
The Critical Role of Carboxy-Terminal Amino Acids in Ligand-Dependent and -Independent Transactivation of the Constitutive Androstane Receptor.
T. Andersin, S. Vaisanen, and C. Carlberg (2003)
Mol. Endocrinol. 17, 234-246
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LXXLL-Related Motifs in Dax-1 Have Target Specificity for the Orphan Nuclear Receptors Ad4BP/SF-1 and LRH-1.
T. Suzuki, M. Kasahara, H. Yoshioka, K.-i. Morohashi, and K. Umesono (2003)
Mol. Cell. Biol. 23, 238-249
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Thyroid Hormone Receptor-{beta} Mutations Conferring Hormone Resistance and Reduced Corepressor Release Exhibit Decreased Stability in the N-Terminal Ligand-Binding Domain.
B. R. Huber, M. Desclozeaux, B. L. West, S. T. Cunha-Lima, H. T. Nguyen, J. D. Baxter, H. A. Ingraham, and R. J. Fletterick (2003)
Mol. Endocrinol. 17, 107-116
   Abstract »    Full Text »    PDF »
Novel Mechanism of Nuclear Receptor Corepressor Interaction Dictated by Activation Function 2 Helix Determinants.
A. N. Moraitis, V. Giguere, and C. C. Thompson (2002)
Mol. Cell. Biol. 22, 6831-6841
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NRC-Interacting Factor 1 Is a Novel Cotransducer That Interacts with and Regulates the Activity of the Nuclear Hormone Receptor Coactivator NRC.
M. A. Mahajan, A. Murray, and H. H. Samuels (2002)
Mol. Cell. Biol. 22, 6883-6894
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Mutations at Positions 547-553 of Rat Glucocorticoid Receptors Reveal That hsp90 Binding Requires the Presence, but Not Defined Composition, of a Seven-amino Acid Sequence at the Amino Terminus of the Ligand Binding Domain.
S. Kaul, P. J. M. Murphy, J. Chen, L. Brown, W. B. Pratt, and S. S. Simons Jr. (2002)
J. Biol. Chem. 277, 36223-36232
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A Structural Model of the Constitutive Androstane Receptor Defines Novel Interactions That Mediate Ligand-Independent Activity.
I. Dussault, M. Lin, K. Hollister, M. Fan, J. Termini, M. A. Sherman, and B. M. Forman (2002)
Mol. Cell. Biol. 22, 5270-5280
   Abstract »    Full Text »    PDF »
Jun Dimerization Protein 2 Functions as a Progesterone Receptor N-Terminal Domain Coactivator.
S. E. Wardell, V. Boonyaratanakornkit, J. S. Adelman, A. Aronheim, and D. P. Edwards (2002)
Mol. Cell. Biol. 22, 5451-5466
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Glucocorticoid Receptor Domain Requirements for Chromatin Remodeling and Transcriptional Activation of the Mouse Mammary Tumor Virus Promoter in Different Nucleoprotein Contexts.
E. K. Keeton, T. M. Fletcher, C. T. Baumann, G. L. Hager, and C. L. Smith (2002)
J. Biol. Chem. 277, 28247-28255
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Direct Interactions between Corepressors and Coactivators Permit the Integration of Nuclear Receptor-Mediated Repression and Activation.
X. Li, E. A. Kimbrel, D. J. Kenan, and D. P. MCDonnell (2002)
Mol. Endocrinol. 16, 1482-1491
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Inhibition of the Dihydrotestosterone-Activated Androgen Receptor by Nuclear Receptor Corepressor.
S. Cheng, S. Brzostek, S. R. Lee, A. N. Hollenberg, and S. P. Balk (2002)
Mol. Endocrinol. 16, 1492-1501
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Cross-repression, a Functional Consequence of the Physical Interaction of Non-liganded Nuclear Receptors and POU Domain Transcription Factors.
M. M. Gonzalez and C. Carlberg (2002)
J. Biol. Chem. 277, 18501-18509
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Characterization of the Retinoid Orphan-Related Receptor-{alpha} Coactivator Binding Interface: A Structural Basis for Ligand-Independent Transcription.
J. M. Harris, P. Lau, S. L. Chen, and G. E. O. Muscat (2002)
Mol. Endocrinol. 16, 998-1012
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The PGC-1-related Protein PERC Is a Selective Coactivator of Estrogen Receptor alpha.
D. Kressler, S. N. Schreiber, D. Knutti, and A. Kralli (2002)
J. Biol. Chem. 277, 13918-13925
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The Nuclear Receptor Coactivators p300/CBP/Cointegrator-Associated Protein (p/CIP) and Transcription Intermediary Factor 2 (TIF2) Differentially Regulate PKA-Stimulated Transcriptional Activity of Steroidogenic Factor 1.
B. Borud, T. Hoang, M. Bakke, A. L. Jacob, J. Lund, and G. Mellgren (2002)
Mol. Endocrinol. 16, 757-773
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The FXXLF Motif Mediates Androgen Receptor-specific Interactions with Coregulators.
B. He, J. T. Minges, L. W. Lee, and E. M. Wilson (2002)
J. Biol. Chem. 277, 10226-10235
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Allosteric Regulation of Estrogen Receptor Structure, Function, and Coactivator Recruitment by Different Estrogen Response Elements.
J. M. Hall, D. P. McDonnell, and K. S. Korach (2002)
Mol. Endocrinol. 16, 469-486
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Ligand-Selective Interactions of ER Detected in Living Cells by Fluorescence Resonance Energy Transfer.
R. V. Weatherman, C.-Y. Chang, N. J. Clegg, D. C. Carroll, R. N. Day, J. D. Baxter, D. P. McDonnell, T. S. Scanlan, and F. Schaufele (2002)
Mol. Endocrinol. 16, 487-496
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TR Surfaces and Conformations Required to Bind Nuclear Receptor Corepressor.
A. Marimuthu, W. Feng, T. Tagami, H. Nguyen, J. L. Jameson, R. J. Fletterick, J. D. Baxter, and B. L. West (2002)
Mol. Endocrinol. 16, 271-286
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The Activating Enzyme of NEDD8 Inhibits Steroid Receptor Function.
M. Fan, X. Long, J. A. Bailey, C. A. Reed, E. Osborne, E. A. Gize, E. A. Kirk, R. M. Bigsby, and K. P. Nephew (2002)
Mol. Endocrinol. 16, 315-330
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Structure-Based Design and Synthesis of a Thyroid Hormone Receptor (TR) Antagonist.
J. D. Baxter, P. Goede, J. W. Apriletti, B. L. West, W. Feng, K. Mellstrom, R. J. Fletterick, R. L. Wagner, P. J. Kushner, R. C. J. Ribeiro, et al. (2002)
Endocrinology 143, 517-524
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AR and ER Interaction with a p21-Activated Kinase (PAK6).
S. R. Lee, S. M. Ramos, A. Ko, D. Masiello, K. D. Swanson, M. L. Lu, and S. P. Balk (2002)
Mol. Endocrinol. 16, 85-99
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Domain Structure of the NRIF3 Family of Coregulators Suggests Potential Dual Roles in Transcriptional Regulation.
D. Li, F. Wang, and H. H. Samuels (2001)
Mol. Cell. Biol. 21, 8371-8384
   Abstract »    Full Text »    PDF »


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