Published in: Molecular and Cellular Biology, vol. 21, no. 13, pp. 4404-4412 (July,  2001):

"Ligand-Mediated Assembly and Real-Time Cellular Dynamics of Estrogen Receptor a-Coactivator Complexes in Living Cells".

David L. Stenoien,1 Anne C. Nye,2 Maureen G. Mancini,1 Kavita Patel,1 Martin Dutertre,1 Bert W. O'Malley,1 Carolyn L. Smith,1 Andrew S. Belmont,2 and Michael A. Mancini 1,*

1 Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, Texas 77030,
2 Department of Cell and Structural Biology, University of Illinois, Urbana-Champaign, Illinois 61801.

* Corresponding author. Mailing address: Department of Molecular and Cellular Biology, Baylor College of Medicine, One BaylorPlaza, Houston, TX 77030. Phone: (713) 798-8952. Fax: (713) 798-8005.
E-mail:  mancini@bcm.tmc.edu.



Abstract:

Studies with live cells demonstrate that agonist and antagonist rapidly (within minutes) modulate the subnuclear dynamics of estrogen receptor a (ER) and steroid receptor coactivator 1 (SRC-1). A functional cyan fluorescent protein (CFP)-tagged lacrepressor-ER chimera (CFP-LacER) was used in live cells to discretelyimmobilize ER on stably integrated lac operator arrays to study recruitment of yellow fluorescent protein (YFP)-steroid receptor coactivators (YFP-SRC-1 and YFP-CREB binding protein [CBP]). In the absence of ligand, YFP-SRC-1 is found dispersed throughout the nucleoplasm, with a surprisingly high accumulation on the CFP-LacER arrays. Agonist addition results in the rapid (within minutes) recruitment of nucleoplasmic YFP-SRC-1, while antagonist additions diminish YFP-SRC-1-CFP-LacER associations. Less ligand-independent colocalization is observed with CFP-LacER and YFP-CBP, but agonist-induced recruitment occurs within minutes. The agonist-induced recruitment of coactivators requires helix 12 and critical residues in the ER-SRC-1 interaction surface, but not the F, AF-1, or DNA binding domains. Fluorescence recovery after photobleaching indicates that YFP-SRC-1, YFP-CBP, and CFP-LacER complexes undergo rapid (within seconds) molecular exchange even in the presence of an agonist. Taken together, these data suggest a dynamic view of receptor-coregulator interactions that is now amenable to real-time study in living cells.



Additional References:

1. "A Steroid Receptor Coactivator, SRA, Functions as an RNA and is present in a SRC-1 Complex".

2. "Activation of DNA Transcription within Repressed Chromatin by Nuclear RNA Species".



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