Hsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor
Hsp chaperones stabilize the inactive conformation of androgen receptor (AR) and are released upon hormone-induced AR activation. Here, the authors locate the Hsp binding region on AR, and show that Hsp70 reduces AR aggregation and promotes AR degradation in cellular and mouse models of a neuromuscu...
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Nature Portfolio
2019
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oai:doaj.org-article:6c6c515e273b446cb66da2f55b7b3d952021-12-02T15:35:54ZHsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor10.1038/s41467-019-11594-y2041-1723https://doaj.org/article/6c6c515e273b446cb66da2f55b7b3d952019-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11594-yhttps://doaj.org/toc/2041-1723Hsp chaperones stabilize the inactive conformation of androgen receptor (AR) and are released upon hormone-induced AR activation. Here, the authors locate the Hsp binding region on AR, and show that Hsp70 reduces AR aggregation and promotes AR degradation in cellular and mouse models of a neuromuscular disorder.Bahareh EftekharzadehVaruna C. BanduseelaGiulio ChiesaPaula Martínez-CristóbalJennifer N. RauchSamir R. NathDaniel M. C. SchwarzHao ShaoMarta Marin-ArganyClaudio Di SanzaElisa GiorgettiZhigang YuRoberta PierattelliIsabella C. FelliIsabelle Brun-HeathJesús GarcíaÁngel R. NebredaJason E. GestwickiAndrew P. LiebermanXavier SalvatellaNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-14 (2019) |
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Science Q Bahareh Eftekharzadeh Varuna C. Banduseela Giulio Chiesa Paula Martínez-Cristóbal Jennifer N. Rauch Samir R. Nath Daniel M. C. Schwarz Hao Shao Marta Marin-Argany Claudio Di Sanza Elisa Giorgetti Zhigang Yu Roberta Pierattelli Isabella C. Felli Isabelle Brun-Heath Jesús García Ángel R. Nebreda Jason E. Gestwicki Andrew P. Lieberman Xavier Salvatella Hsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor |
description |
Hsp chaperones stabilize the inactive conformation of androgen receptor (AR) and are released upon hormone-induced AR activation. Here, the authors locate the Hsp binding region on AR, and show that Hsp70 reduces AR aggregation and promotes AR degradation in cellular and mouse models of a neuromuscular disorder. |
format |
article |
author |
Bahareh Eftekharzadeh Varuna C. Banduseela Giulio Chiesa Paula Martínez-Cristóbal Jennifer N. Rauch Samir R. Nath Daniel M. C. Schwarz Hao Shao Marta Marin-Argany Claudio Di Sanza Elisa Giorgetti Zhigang Yu Roberta Pierattelli Isabella C. Felli Isabelle Brun-Heath Jesús García Ángel R. Nebreda Jason E. Gestwicki Andrew P. Lieberman Xavier Salvatella |
author_facet |
Bahareh Eftekharzadeh Varuna C. Banduseela Giulio Chiesa Paula Martínez-Cristóbal Jennifer N. Rauch Samir R. Nath Daniel M. C. Schwarz Hao Shao Marta Marin-Argany Claudio Di Sanza Elisa Giorgetti Zhigang Yu Roberta Pierattelli Isabella C. Felli Isabelle Brun-Heath Jesús García Ángel R. Nebreda Jason E. Gestwicki Andrew P. Lieberman Xavier Salvatella |
author_sort |
Bahareh Eftekharzadeh |
title |
Hsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor |
title_short |
Hsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor |
title_full |
Hsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor |
title_fullStr |
Hsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor |
title_full_unstemmed |
Hsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor |
title_sort |
hsp70 and hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor |
publisher |
Nature Portfolio |
publishDate |
2019 |
url |
https://doaj.org/article/6c6c515e273b446cb66da2f55b7b3d95 |
work_keys_str_mv |
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