Steroid receptors (SRs) encompass a family of transcription factors that regulate the expression of thousands of genes upon binding to steroid hormones and include the glucocorticoid, androgen, progesterone, estrogen and mineralocorticoid receptors. SRs control key physiological and pathological processes, thus becoming relevant drug targets. As with many other nuclear proteins, hormone-activated SRs concentrate in multiple discrete foci within the cell nucleus. Even though these foci were first observed ∼25 years ago, their exact structure and function remained elusive. In the last years, new imaging methodologies and theoretical frameworks improved our understanding of the intranuclear organization. These studies led to a new paradigm stating that many membraneless nuclear compartments, including transcription-related foci, form through a liquid–liquid phase separation process. These exciting ideas impacted the SR field by raising the hypothesis of SR foci as liquid condensates involved in transcriptional regulation. In this work, we review the current knowledge about SR foci formation under the light of the condensate model, analyzing how these structures may impact SR function. These new ideas, combined with state-of-the-art techniques, may shed light on the biophysical mechanisms governing the formation of SR foci and the biological function of these structures in normal physiology and disease.
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January 2021
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High protein levels of protein kinase C confer a survival advantage in many cancers, including pancreatic cancer. In this issue, Tovell and Newton (pp. 341–355) review the mechanisms controlling the stability of protein kinase C, focusing on negative regulation by the phosphatase PHLPP as a potential strategy to restore protein levels of the kinase. Image provided by Hannah Tovell and was created with BioRender.com.
Review Article|
January 29 2021
Phasing the intranuclear organization of steroid hormone receptors
Martin Stortz;
Martin Stortz
*
1Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales (IQUIBICEN), CONICET-Universidad de Buenos Aires, Facultad de Ciencias Exactas y Naturales, Buenos Aires C1428EGA, Argentina
2Departamento de Fisiología, Biología Molecular y Celular, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires C1428EGA, Argentina
Correspondence: Martin Stortz (mstortz@qb.fcen.uba.ar) or Diego M. Presman (presmandm@fbmc.fcen.uba.ar) or Adali Pecci (apecci@qb.fcen.uba.ar) or Valeria Levi (vlevi12@gmail.com)
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Diego M. Presman
;
Diego M. Presman
*
3Instituto de Fisiología, Biología Molecular y Neurociencias (IFIBYNE), CONICET-Universidad de Buenos Aires, Facultad de Ciencias Exactas y Naturales, Buenos Aires C1428EGA, Argentina
Correspondence: Martin Stortz (mstortz@qb.fcen.uba.ar) or Diego M. Presman (presmandm@fbmc.fcen.uba.ar) or Adali Pecci (apecci@qb.fcen.uba.ar) or Valeria Levi (vlevi12@gmail.com)
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Adali Pecci;
3Instituto de Fisiología, Biología Molecular y Neurociencias (IFIBYNE), CONICET-Universidad de Buenos Aires, Facultad de Ciencias Exactas y Naturales, Buenos Aires C1428EGA, Argentina
4Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires C1428EGA, Argentina
Correspondence: Martin Stortz (mstortz@qb.fcen.uba.ar) or Diego M. Presman (presmandm@fbmc.fcen.uba.ar) or Adali Pecci (apecci@qb.fcen.uba.ar) or Valeria Levi (vlevi12@gmail.com)
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Valeria Levi
Valeria Levi
†
1Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales (IQUIBICEN), CONICET-Universidad de Buenos Aires, Facultad de Ciencias Exactas y Naturales, Buenos Aires C1428EGA, Argentina
4Departamento de Química Biológica, Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Buenos Aires C1428EGA, Argentina
Correspondence: Martin Stortz (mstortz@qb.fcen.uba.ar) or Diego M. Presman (presmandm@fbmc.fcen.uba.ar) or Adali Pecci (apecci@qb.fcen.uba.ar) or Valeria Levi (vlevi12@gmail.com)
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Publisher: Portland Press Ltd
Received:
November 09 2020
Revision Received:
December 28 2020
Accepted:
January 07 2021
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 2021 The Author(s). Published by Portland Press Limited on behalf of the Biochemical Society
2021
Biochem J (2021) 478 (2): 443–461.
Article history
Received:
November 09 2020
Revision Received:
December 28 2020
Accepted:
January 07 2021
Citation
Martin Stortz, Diego M. Presman, Adali Pecci, Valeria Levi; Phasing the intranuclear organization of steroid hormone receptors. Biochem J 29 January 2021; 478 (2): 443–461. doi: https://doi.org/10.1042/BCJ20200883
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