FRAP reveals that mobility of oestrogen receptor-α is ligand- and proteasome-dependent

被引:335
作者
Stenoien, DL [1 ]
Patel, K [1 ]
Mancini, MG [1 ]
Dutertre, M [1 ]
Smith, CL [1 ]
O'Malley, BW [1 ]
Mancini, MA [1 ]
机构
[1] Baylor Coll Med, Dept Mol & Cellular Biol, Houston, TX 77030 USA
关键词
D O I
10.1038/35050515
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Here we report the use of fluorescence recovery after photobleaching (FRAP) to examine the intranuclear dynamics of fluorescent oestrogen receptor-alpha (ER). After bleaching, unliganded ER exhibits high mobility (recovery t(1/2) < 1 s). Agonist (oestradiol; E2) or partial antagonist (4-hydroxytamoxifen) slows ER recovery (t(1/2) <similar to>5-6 s), whereas the pure antagonist (ICI 182,780) and, surprisingly, proteasome inhibitors each immobilize ER to the nuclear matrix. Dual FRAP experiments show that fluorescent ER and SRC-1 exhibit similar dynamics only in the presence of E2. In contrast to reports that several nuclear proteins show uniform dynamics, ER exhibits differential mobility depending upon several factors that ave linked to its transcription function.
引用
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页码:15 / 23
页数:9
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