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Multiple exportins influence thyroid hormone receptor localization.

Kelly S Subramanian1, Rose C Dziedzic1, Hallie N Nelson1

  • 1Department of Biology, College of William and Mary, Williamsburg, Virginia 23185, USA.

Molecular and Cellular Endocrinology
|April 26, 2015
PubMed
Summary
This summary is machine-generated.

Thyroid hormone receptor (TR) export from the nucleus involves more than one pathway. Multiple exportins, not just CRM1, regulate TR shuttling, impacting its function in metabolism and development.

Keywords:
ExportinNuclear exportThyroid hormoneThyroid hormone receptor

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Endocrinology

Background:

  • Thyroid hormone receptor (TR) plays a crucial role in regulating genes for metabolism and development.
  • TR shuttles between the nucleus and cytoplasm, a process vital for its function.
  • Previous studies identified a CRM1/calreticulin-mediated nuclear export pathway for TR.

Purpose of the Study:

  • To investigate if additional nuclear export pathways, beyond CRM1, are involved in thyroid hormone receptor (TR) nucleocytoplasmic shuttling.
  • To identify other exportins that may regulate TR localization and function.

Main Methods:

  • Utilized RNA interference (RNAi) to knock down specific exportin proteins in transfected cells.
  • Employed fluorescence recovery after photobleaching (FRAP) assays to monitor TR shuttling dynamics.
  • Assessed the impact of exportin modulation on TR-responsive reporter gene transactivation.

Main Results:

  • Knockdown of exportins 4, 5, and 7 significantly altered TR shuttling dynamics.
  • Overexpression of exportins 5 and 7 led to a noticeable shift of TR distribution towards the cytosol.
  • Modulation of exportin levels affected the transactivation activity of the TR-responsive reporter gene.

Conclusions:

  • Multiple exportins, in addition to CRM1, actively participate in regulating thyroid hormone receptor (TR) nucleocytoplasmic shuttling.
  • A complex interplay between nuclear import, retention, and multiple export pathways fine-tunes TR localization and function.
  • These findings reveal a more intricate mechanism controlling TR activity than previously understood.