Cytoplasm-to-nucleus shuttling of thyroid hormone receptor-β1 (TRβ1) is directed from a plasma membrane integrin receptor by thyroid hormone

H. James Cao, Hung Yun Lin, Mary K. Luidens, Faith B. Davis, Paul J. Davis

Research output: Contribution to journalArticle

31 Citations (Scopus)

Abstract

Introduction. In CV-1 cells, shuttling from cytoplasm to nucleus of the nuclear thyroid hormone receptor-01 (TB/31, TR) is shown in this report to be regulated by extracellular thyroid hormone at a hormone receptor on cell surface integrin av3. Methods. The receptor was introduced into cells as a GFP-TR1 chimera and intracellular movement of the receptor was monitored by confocal microscopy of cells treated with L-thyroxine (T 4). Results and Discussion. TR-GFP translocation in the presence ofT 4 requires activation of extracellular-regulated protein kinases 1/2 (ERK1/2). Inhibition of Tj-binding to av/33 with anti-av/33 or Arg-Gly-Asp (RGD) peptide blocks TfStimulated GFP-TR nuclear translocation, as do the hormone-binding inhibitor tetraiodothyroacetic acid (tet-rac) and the ERK1/2 inhibitor, PD98059. TR1 is an ERK1/2 substrate. Conclusions. Via a nongenomic mechanism initiated at plasma membrane integrin v3, T 2a-activated ERK1/2 and TR1 move transiently in an immunoprecipitable comphx to the nuclei of T 2a-treated cells.

Original languageEnglish
Pages (from-to)31-42
Number of pages12
JournalEndocrine Research
Volume34
Issue number1-2
DOIs
Publication statusPublished - Mar 2009
Externally publishedYes

Keywords

  • Integrin αvβ3
  • L-thyroxine
  • Nongenomic Actions
  • TRβ1 Transport

ASJC Scopus subject areas

  • Endocrinology

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