Literature DB >> 34061186

Steroid receptor-coregulator transcriptional complexes: new insights from CryoEM.

Ping Yi1, Xinzhe Yu2, Zhao Wang1,2, Bert W O'Malley1.   

Abstract

Steroid receptors activate gene transcription through recruitment of a number of coregulators to facilitate histone modification, chromatin remodeling, and general transcription machinery stabilization. Understanding the structures of full-length steroid receptor and coregulatory complexes has been difficult due to their large molecular sizes and dynamic structural conformations. Recent developments in cryo-electron microscopy (cryoEM) technology and proteomics have advanced the structural studies of steroid receptor complexes. Here, we will review the insights we learned from cryoEM studies of the estrogen and androgen receptor transcriptional complexes. Despite similar domain organizations, the two receptors have different coregulator interaction modes. The cryoEM structures now have revealed the fundamental differences between the two receptors and their functional mechanisms.
© 2021 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society.

Entities:  

Keywords:  androgen; cryo-electron microscopy; estrogen; nuclear receptors; structural studies; transcription

Mesh:

Substances:

Year:  2021        PMID: 34061186      PMCID: PMC8845409          DOI: 10.1042/EBC20210019

Source DB:  PubMed          Journal:  Essays Biochem        ISSN: 0071-1365            Impact factor:   8.000


  59 in total

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Journal:  J Biol Chem       Date:  2002-05-08       Impact factor: 5.157

2.  Crosstalk between CARM1 methylation and CBP acetylation on histone H3.

Authors:  Sylvain Daujat; Uta-Maria Bauer; Vanya Shah; Bryan Turner; Shelley Berger; Tony Kouzarides
Journal:  Curr Biol       Date:  2002-12-23       Impact factor: 10.834

3.  Molecular basis of agonism and antagonism in the oestrogen receptor.

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Journal:  Nature       Date:  1997-10-16       Impact factor: 49.962

4.  Proteomic analysis of coregulators bound to ERα on DNA and nucleosomes reveals coregulator dynamics.

Authors:  Charles E Foulds; Qin Feng; Chen Ding; Suzanna Bailey; Tamra L Hunsaker; Anna Malovannaya; Ross A Hamilton; Leah A Gates; Zheng Zhang; Chunshu Li; Doug Chan; Amol Bajaj; Celetta G Callaway; Dean P Edwards; David M Lonard; Sophia Y Tsai; Ming-Jer Tsai; Jun Qin; Bert W O'Malley
Journal:  Mol Cell       Date:  2013-07-11       Impact factor: 17.970

5.  Stepwise androgen receptor dimerization.

Authors:  Martin E van Royen; Wiggert A van Cappellen; Carola de Vos; Adriaan B Houtsmuller; Jan Trapman
Journal:  J Cell Sci       Date:  2012-02-10       Impact factor: 5.285

6.  Structure of the intact PPAR-gamma-RXR- nuclear receptor complex on DNA.

Authors:  Vikas Chandra; Pengxiang Huang; Yoshitomo Hamuro; Srilatha Raghuram; Yongjun Wang; Thomas P Burris; Fraydoon Rastinejad
Journal:  Nature       Date:  2008-11-20       Impact factor: 49.962

7.  Domains of the human androgen receptor involved in steroid binding, transcriptional activation, and subcellular localization.

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Journal:  Mol Endocrinol       Date:  1991-10

8.  H3R42me2a is a histone modification with positive transcriptional effects.

Authors:  Fabio Casadio; Xiangdong Lu; Samuel B Pollock; Gary LeRoy; Benjamin A Garcia; Tom W Muir; Robert G Roeder; C David Allis
Journal:  Proc Natl Acad Sci U S A       Date:  2013-08-26       Impact factor: 11.205

9.  Estrogen receptor activation function 1 works by binding p160 coactivator proteins.

Authors:  P Webb; P Nguyen; J Shinsako; C Anderson; W Feng; M P Nguyen; D Chen; S M Huang; S Subramanian; E McKinerney; B S Katzenellenbogen; M R Stallcup; P J Kushner
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Review 10.  The nuclear receptor superfamily: A structural perspective.

Authors:  Emily R Weikum; Xu Liu; Eric A Ortlund
Journal:  Protein Sci       Date:  2018-11       Impact factor: 6.725

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  1 in total

1.  Nuclear receptors: from molecular mechanisms to therapeutics.

Authors:  Daniel E Frigo; Maria Bondesson; Cecilia Williams
Journal:  Essays Biochem       Date:  2021-12-17       Impact factor: 8.000

  1 in total

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