Nishi · Methods in molecular biology (Clifton, N.J.) 2010 · In vitro live-cell fluorescence imaging study · n=?

Imaging of transcription factor trafficking in living cells: lessons from corticosteroid receptor dynamics.

Cited 17 times in the scientific literature.

Level 5 - mechanism / opinion, no new human data

In vitro bench imaging research and methodological book chapter (CEBM Level 5).

PubMed 20694669 · doi:10.1007/978-1-60761-738-9_12 · record verified 2026-08-30

What was done

Live-cell fluorescence microscopy techniques were applied to track the subcellular trafficking and interactions of green fluorescent protein (GFP)-labeled glucocorticoid receptors (GR) and mineralocorticoid receptors (MR) following corticosterone (CORT) treatment. The investigations evaluated: (1) time-lapse imaging of receptor translocation from the cytoplasm to the nucleus across varying CORT concentrations, (2) intranuclear receptor mobility using fluorescence recovery after photobleaching (FRAP), and (3) GR-MR heterodimer formation using fluorescence resonance energy transfer (FRET).

What was found

Both GR and MR translocated from the cytoplasm to the nucleus after CORT treatment, with the time course depending on CORT concentration. FRAP analysis showed that liganded GR and MR in the nucleus were highly mobile rather than trapped by specific organelles. FRET analysis detected GR-MR heterodimers influenced by changing CORT concentrations. The abstract provides no exact numerical values, kinetics, or statistical parameters.

Why it matters

Understanding the real-time translocation, intranuclear mobility, and heterodimerization of GR and MR provides mechanistic insights into how dynamic hormone fluctuations—such as circadian rhythms or acute stress—regulate transcriptional responses in neural cells.

Limits

This is an in vitro methodological chapter without human or in vivo data. The abstract does not specify the host cell lines, sample sizes, kinetic rates, or statistical significance, and GFP-tagged overexpression models may not fully recapitulate endogenous receptor physiology.

Cited by