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Molecular Endocrinology 14 (12): 2024-2039
Copyright © 2000 by The Endocrine Society

Temporally Distinct and Ligand-Specific Recruitment of Nuclear Receptor-Interacting Peptides and Cofactors to Subnuclear Domains Containing the Estrogen Receptor

Fred Schaufele, Ching-yi Chang, Weiqun Liu, John D. Baxter1, Steven K. Nordeen, Yihong Wan, Richard N. Day and Donald P. McDonnell

Metabolic Research Unit and Department of Medicine (F.S., W.L., J.D.B.) University of California San Francisco, California 94143
Department of Pharmacology and Cancer Biology (C.-y.C., D.P.M.) Duke University Medical Center Durham, North Carolina 27710
Department of Pathology and Program in Molecular Biology (S.K.N., Y.W.) University of Colorado Health Sciences Center Denver, Colorado 80262 Departments of Medicine and Cell Biology (R.N.D.) National Science Foundation Center for Biological Timing University of Virginia Health Sciences Center Charlottesville, Virginia, 22908

Ligand binding to estrogen receptor (ER) is presumed to regulate the type and timing of ER interactions with different cofactors. Using fluorescence microscopy in living cells, we characterized the recruitment of five different green fluorescent protein (GFP)-labeled ER-interacting peptides to the distinct subnuclear compartment occupied by blue fluorescent protein (BFP)-labeled ER{alpha}. Different ligands promoted the recruitment of different peptides. One peptide was recruited in response to estradiol (E2), tamoxifen, raloxifene, or ICI 182,780 incubation whereas other peptides were recruited specifically by E2 or tamoxifen. Peptides containing different sequences surrounding the ER-interacting motif LXXLL were recruited with different time courses after E2 addition. Complex temporal kinetics also were observed for recruitment of the full-length, ER cofactor glucocorticoid receptor-interacting protein 1 (GRIP1); rapid, E2-dependent recruitment of GRIP1 was blocked by mutation of the GRIP1 LXXLL motifs to LXXAA whereas slower E2 recruitment persisted for the GRIP1 LXXAA mutant. This suggested the presence of multiple, temporally distinct GRIP 1 recruitment mechanisms. E2 recruitment of GRIP1 and LXXLL peptides was blocked by coincubation with excess ICI 182,780. In contrast, preformed E2/ER/GRIP1 and E2/ER/LXXLL complexes were resistant to subsequent ICI 182,780 addition whereas ICI 182,780 dispersed preformed complexes containing the GRIP1 LXXAA mutant. This suggested that E2-induced LXXLL binding altered subsequent ligand/ER interactions. Thus, alternative, ligand-selective recruitment and dissociation mechanisms with distinct temporal sequences are available for ER{alpha} action in vivo.




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