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and Steroid Receptor Coactivator-1
Department of Molecular and Cellular Biology (D.L.S., M.G.M., K.P.,
C.L.S., M.A.M.) Baylor College of Medicine Houston, Texas
77030
Ligand Pharmaceuticals, Inc. (E.A.A.)
San Diego, California 92121
We have *analyzed ligand-dependent, subnuclear
movements of the estrogen receptor-
(ER) in terms of both spatial
distribution and solubility partitioning. Using a transcriptionally
active green fluorescent protein-ER chimera (GFP-ER), we find
that 17ß-estradiol (E2) changes the normally
diffuse nucleoplasmic pattern of GFP-ER to a hyperspeckled
distribution within 10–20 min. A similar reorganization occurs with
the partial antagonist 4-hydroxytamoxifen; only a subtle effect was
observed with the pure antagonist ICI 182,780. To examine the influence
of ligand upon ER association with nuclear structure, MCF-7 cells
were extracted to reveal the nuclear matrix (NM). Addition of
E2, 4-hydroxytamoxifen, or ICI 182,780
causes ER to partition with the NM-bound fraction on a similar time
course (10–20 min) as the spatial reorganization suggesting that the
two events are related. To determine the effects of
E2 on the redistribution and solubility of
GFP-ER, individual cells were directly examined during both hormone
addition and NM extraction and showed that GFP-ER movement and NM
association were coincident. Colocalization experiments were performed
with antibodies to identify sites of transcription (RNA pol IIo) and
splicing domains (SRm160). Using E2 treated
MCF-7 cells, minor overlap was observed with transcription sites and a
small amount of the total ER pool. Experiments performed with
bioluminescent derivatives of ER and steroid receptor
coactivator-1 (SRC-1) demonstrated both proteins colocalize to the same
NM-bound foci in response to E2 but not the
antagonists tested. Deletion mutagenesis and in situ
analyses indicate intranuclear colocalization requires a central SRC-1
domain containing LXXLL motifs. Collectively, our data suggest that
ER transcription function is dependent upon dynamic early events
including intranuclear rearrangement, NM association, and SRC-1
interactions.
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H. Zhang, L. Liao, S.-Q. Kuang, and J. Xu Spatial Distribution of the Messenger Ribonucleic Acid and Protein of the Nuclear Receptor Coactivator, Amplified in Breast Cancer-3, in Mice Endocrinology, April 1, 2003; 144(4): 1435 - 1443. [Abstract] [Full Text] [PDF]
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M. J. M. Schaaf and J. A. Cidlowski Molecular Determinants of Glucocorticoid Receptor Mobility in Living Cells: the Importance of Ligand Affinity Mol. Cell. Biol., March 15, 2003; 23(6): 1922 - 1934. [Abstract] [Full Text] [PDF]
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K.-i. Matsuda, I. Ochiai, M. Nishi, and M. Kawata Colocalization and Ligand-Dependent Discrete Distribution of the Estrogen Receptor (ER){alpha} and ER{beta} Mol. Endocrinol., October 1, 2002; 16(10): 2215 - 2230. [Abstract] [Full Text] [PDF]
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 J.-B. Lazaro, P. J. Bailey, and A. B. Lassar Cyclin D-cdk4 activity modulates the subnuclear localization and interaction of MEF2 with SRC-family coactivators during skeletal muscle differentiation Genes & Dev., July 15, 2002; 16(14): 1792 - 1805. [Abstract] [Full Text] [PDF]
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