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Nuclear Cytoplasmic Shuttling by Thyroid Hormone Receptors

Journal of Biological Chemistry, ISSN: 0021-9258, Vol: 276, Issue: 14, Page: 11237-11245
2001
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Article Description

In this report, we have studied the intracellular dynamics and distribution of the thyroid hormone receptor-β (TRβ) in living cells, utilizing fusions to the green fluorescent protein. Wild-type TRβ was mostly nuclear in both the absence and presence of triiodothyronine; however, triiodothyronine induced a nuclear reorganization of TRβ. By mutating defined regions of TRβ, we found that both nuclear corepressor and retinoid X receptor are involved in maintaining the unliganded receptor within the nucleus. A TRβ mutant defective in DNA binding had only a slightly altered nuclear/cytoplasmic distribution compared with wild-type TRβ; thus, site-specific DNA binding is not essential for maintaining TRβ within the nucleus. Both ATP depletion studies and heterokaryon analysis demonstrated that TRβ rapidly shuttles between the nuclear and the cytoplasmic compartments. Cotransfection of nuclear corepressor and retinoid X receptor markedly decreased the shuttling by maintaining unliganded TRβ within the nucleus. In summary, our findings demonstrate that TRβ rapidly shuttles between the nucleus and the cytoplasm and that protein-protein interactions of TRβ with various cofactors, rather than specific DNA interactions, play the predominant role in determining the intracellular distribution of the receptor.

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