Intranuclear mobility of estrogen receptor alpha and progesterone receptors in association with nuclear matrix dynamics.

We analyzed the intranuclear dynamics of estrogen receptor alpha (ER alpha) and progesterone receptor (PR)-A/B labeled with different spectral variants of green fluorescent protein (GFP) in living cells. The distribution of ER alpha 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 ER alpha. The nuclear areas where PR-A/B were accumulated were colocalized with the cluster of ER alpha, 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 ER alpha, while the mobility of ER alpha 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 ER alpha. By ATP-depletion from the cells, most of ER alpha 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 ER alpha and PR-A/B, showed ATP-dependent rapid exchange in the nucleus. These results indicate that the mobility of ER alpha and PR-A/B is associated with the dynamics of the nuclear matrix. Copyright (c) 2007 Wiley-Liss, Inc.