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Intranuclear mobility of estrogen receptor α and progesterone receptors in association with nuclear matrix dynamics
Author(s) -
Matsuda KenIchi,
Nishi Mayumi,
Takaya Hisamitsu,
Kaku Natsuko,
Kawata Mitsuhiro
Publication year - 2007
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.21393
Subject(s) - nuclear matrix , estrogen receptor , fluorescence recovery after photobleaching , progesterone receptor , nuclear receptor , nuclear transport , cell nucleus , nuclear protein , chemistry , receptor , matrix (chemical analysis) , nucleus , biology , microbiology and biotechnology , transcription factor , biochemistry , gene , chromatin , genetics , chromatography , cancer , membrane , breast cancer
We analyzed the intranuclear dynamics of estrogen receptor α (ERα) and progesterone receptor (PR)‐A/B labeled with different spectral variants of green fluorescent protein (GFP) in living cells. The distribution of ERα and PR‐A/B were changed from a diffuse to discrete pattern after the addition of both ligands, but the extent of discrete cluster formation of PR‐A/B was lower than that of ERα. The nuclear areas where PR‐A/B were accumulated were colocalized with the cluster of ERα, suggesting that cross‐talk in the transcriptional regulation occurred in the loci. Fluorescence recovery after photobleaching (FRAP) analysis revealed that the mobility of PR‐A/B was hastened by the coexistence of ERα, while the mobility of ERα was not changed by the coexistence of PR‐A/B. Cluster formation was correlated with the nuclear matrix binding, because nuclear matrix binding capacity was also lower in PR‐A/B than ERα. By ATP‐depletion from the cells, most of ERα and PR‐A/B were bound to the nuclear matrix and their mobilities were extinguished both in the absence and presence of ligand. Fluorescent protein (FP) tagged nuclear matrix component protein (NuMA), which was colocalized with ERα and PR‐A/B, showed ATP‐dependent rapid exchange in the nucleus. These results indicate that the mobility of ERα and PR‐A/B is associated with the dynamics of the nuclear matrix. J. Cell. Biochem. 103: 136–148, 2008. © 2007 Wiley‐Liss, Inc.