About this item:

55 Views | 23 Downloads

Author Notes:

Correspondence to E.A.O. and K.R.Y. eortlun@emory.edu; yamamoto@ucsf.edu

The authors thank the members of the Yamamoto laboratory for critical reading of the manuscript, with special note to Elaine Kirschke for insightful discussions, Samantha Cooper, Sheng-Hong Chen and Benjamin Schiller for use of unpublished data, and Kirk Ehmsen for use of unpublished data and assistance with Figure 3.

The authors declare no competing interests.

Subject:

Research Funding:

E.R.W. is supported by US National Institutes of Health (NIH) predoctoral National Research Service Award (NRSA) 1 G31 GM 113397–01A1 from the National Institute of General Medical Sciences.

M.T.K. is supported by NIH postdoctoral NRSA 5T32HL007731–20 from the National Heart, Lung, and Blood Institute and by NIH grant R01CA020535 from the National Cancer Institute.

E.A.O. is supported by NIH grant R01DK095750 from the National Institute of Diabetes and Digestive and Kidney Diseases, by American Heart Association (AHA) grant 14GRNT20460124 and by a W.M. Keck Foundation Medical Research Grant.

K.R.Y. is supported by NIH grants R01CA020535 from the National Cancer Institute and R21ES026068 from the National Institute of Environmental Health Sciences, and by grant MCB-161 5826 from the National Science Foundation.

Keywords:

  • Science & Technology
  • Life Sciences & Biomedicine
  • Cell Biology
  • LIGAND-BINDING DOMAIN
  • NUCLEAR HORMONE-RECEPTORS
  • FACTOR-KAPPA-B
  • SUMO-SMRT/NCOR1-HDAC3 REPRESSING COMPLEX
  • HISTONE ACETYLTRANSFERASE COMPLEXES
  • SITE-SPECIFIC PHOSPHORYLATION
  • CHROMATIN REMODELING COMPLEX
  • ACTIVATION DOMAIN
  • DNA-BINDING
  • GENE-EXPRESSION

Glucocorticoid receptor control of transcription: precision and plasticity via allostery

Tools:

Journal Title:

Nature Reviews Molecular Cell Biology

Volume:

Volume 18, Number 3

Publisher:

, Pages 159-174

Type of Work:

Article | Post-print: After Peer Review

Abstract:

The glucocorticoid receptor (GR) is a constitutively expressed transcriptional regulatory factor (TRF) that controls many distinct gene networks, each uniquely determined by particular cellular and physiological contexts. The precision of GR-mediated responses seems to depend on combinatorial, context-specific assembly of GR-nucleated transcription regulatory complexes at genomic response elements. In turn, evidence suggests that context-driven plasticity is conferred by the integration of multiple signals, each serving as an allosteric effector of GR conformation, a key determinant of regulatory complex composition and activity. This structural and mechanistic perspective on GR regulatory specificity is likely to extend to other eukaryotic TRFs.

Copyright information:

© 2017 Macmillan Publishers Limited, part of Springer Nature. All rights reserved.

Export to EndNote