Hsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptor

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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Main Authors: 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
Format: Article
Language:English
Published: Nature Publishing Group 2019-08-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-019-11594-y
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spelling doaj-6c6c515e273b446cb66da2f55b7b3d952021-05-11T12:02:15ZengNature Publishing GroupNature Communications2041-17232019-08-0110111410.1038/s41467-019-11594-yHsp70 and Hsp40 inhibit an inter-domain interaction necessary for transcriptional activity in the androgen receptorBahareh Eftekharzadeh0Varuna C. Banduseela1Giulio Chiesa2Paula Martínez-Cristóbal3Jennifer N. Rauch4Samir R. Nath5Daniel M. C. Schwarz6Hao Shao7Marta Marin-Argany8Claudio Di Sanza9Elisa Giorgetti10Zhigang Yu11Roberta Pierattelli12Isabella C. Felli13Isabelle Brun-Heath14Jesús García15Ángel R. Nebreda16Jason E. Gestwicki17Andrew P. Lieberman18Xavier Salvatella19Institute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyDepartment of Pathology, University of MichiganInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyUniversity of California at San Francisco, Department of Pharmaceutical ChemistryDepartment of Pathology, University of MichiganUniversity of California at San Francisco, Department of Pharmaceutical ChemistryUniversity of California at San Francisco, Department of Pharmaceutical ChemistryInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyDepartment of Pathology, University of MichiganDepartment of Pathology, University of MichiganCERM and Department of Chemistry “Ugo Schiff”, University of FlorenceCERM and Department of Chemistry “Ugo Schiff”, University of FlorenceInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyUniversity of California at San Francisco, Department of Pharmaceutical ChemistryDepartment of Pathology, University of MichiganInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and TechnologyHsp 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.https://doi.org/10.1038/s41467-019-11594-y
collection DOAJ
language English
format Article
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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
spellingShingle 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
Nature Communications
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 Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2019-08-01
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.
url https://doi.org/10.1038/s41467-019-11594-y
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