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Analysis of intranuclear binding process of glucocorticoid receptor using fluorescence correlation spectroscopy
Author(s) -
Mikuni Shintaro,
Tamura Mamoru,
Kinjo Masataka
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.12.038
Subject(s) - glucocorticoid receptor , fluorescence correlation spectroscopy , chemistry , biophysics , fluorescence spectroscopy , fluorescence , nuclear magnetic resonance , receptor , biochemistry , biology , physics , optics , molecule , organic chemistry
The diffusion properties of EGFP‐hGRα and mutants C421G, A458T and I566 in living cells were analyzed. The wild type and mutants C421G and A458T translocated from the cytoplasm to the nucleus after addition of Dex; however, the Brownian motions of the proteins were different. The diffusion constant of wild‐type GRα after addition of Dex slowed to 15.6% of that in the absence of Dex, whereas those of A458T and C421G slowed to 34.8% and 61.7%, respectively. This is the first report that dimer formation is less important than the binding activity of GRα to GRE in the living cell.