Journal
NATURE CELL BIOLOGY
Volume 3, Issue 1, Pages 15-23Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/35050515
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Funding
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [R01DK053002, F32DK009787, R01DK055622] Funding Source: NIH RePORTER
- NIDDK NIH HHS [R01 DK53002, 1F3DK09787, R01 DK55622] Funding Source: Medline
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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) 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.
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