FRAP reveals that mobility of oestrogen receptor-alpha is ligand- and proteasome-dependent.
作者： David L. Stenoien , Kavita Patel , Maureen G. Mancini , Martin Dutertre , Carolyn L. Smith
DOI: 10.1038/35050515
关键词:
摘要: Here we report the use of fluorescence recovery after photobleaching (FRAP) to examine intranuclear dynamics fluorescent oestrogen receptor-alpha (ER). After bleaching, unliganded ER exhibits high mobility (recovery t1/2 < 1 s). Agonist (oestradiol; E2) or partial antagonist (4-hydroxytamoxifen) slows (t1/2 approximately 5-6 s), whereas pure (ICI 182,780) and, surprisingly, proteasome inhibitors each immobilize nuclear matrix. Dual FRAP experiments show that and SRC-1 exhibit similar only in presence E2. In contrast reports several proteins uniform dynamics, differential depending upon factors are linked its transcription function.
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