Cargando…
HDAC6–ubiquitin interaction controls the duration of HSF1 activation after heat shock
After heat shock, HSF1 controls a major cellular transcriptional response involving the activation of early (HSP70) and late (HSP25) heat shock gene expression. Here we show that a full response to heat shock (activation of both HSP70 and HSP25) depends on the duration of HSF1 activation, which is i...
Autores principales: | , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2014
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4263459/ https://www.ncbi.nlm.nih.gov/pubmed/25298398 http://dx.doi.org/10.1091/mbc.E14-06-1032 |
_version_ | 1782348574892228608 |
---|---|
author | Pernet, Lydia Faure, Virginie Gilquin, Benoit Dufour-Guérin, Solenne Khochbin, Saadi Vourc’h, Claire |
author_facet | Pernet, Lydia Faure, Virginie Gilquin, Benoit Dufour-Guérin, Solenne Khochbin, Saadi Vourc’h, Claire |
author_sort | Pernet, Lydia |
collection | PubMed |
description | After heat shock, HSF1 controls a major cellular transcriptional response involving the activation of early (HSP70) and late (HSP25) heat shock gene expression. Here we show that a full response to heat shock (activation of both HSP70 and HSP25) depends on the duration of HSF1 activation, which is itself controlled by HDAC6, a unique deacetylase known to bind monoubiquitin and polyubiquitin with high affinity. On the basis of a comparative analysis of the heat shock response in cells knocked out for HDAC6 or expressing HDAC6 mutants, we show that HDAC6 binding to ubiquitinated proteins controls the duration of HSF1 activation after heat shock. In cells expressing HDAC6 mutated in the ubiquitin-binding domain, the AAA ATPase factor p97/VCP mediates rapid inactivation of HSF1, precluding late activation of the HSP25 gene. In these cells, knockdown of p97/VCP rescues HSF1 from this rapid inactivation and restores HSP25 expression. We present here a new regulatory circuit that adjusts the duration of the heat shock response to the extent of protein ubiquitination after heat shock. |
format | Online Article Text |
id | pubmed-4263459 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | The American Society for Cell Biology |
record_format | MEDLINE/PubMed |
spelling | pubmed-42634592015-03-02 HDAC6–ubiquitin interaction controls the duration of HSF1 activation after heat shock Pernet, Lydia Faure, Virginie Gilquin, Benoit Dufour-Guérin, Solenne Khochbin, Saadi Vourc’h, Claire Mol Biol Cell Articles After heat shock, HSF1 controls a major cellular transcriptional response involving the activation of early (HSP70) and late (HSP25) heat shock gene expression. Here we show that a full response to heat shock (activation of both HSP70 and HSP25) depends on the duration of HSF1 activation, which is itself controlled by HDAC6, a unique deacetylase known to bind monoubiquitin and polyubiquitin with high affinity. On the basis of a comparative analysis of the heat shock response in cells knocked out for HDAC6 or expressing HDAC6 mutants, we show that HDAC6 binding to ubiquitinated proteins controls the duration of HSF1 activation after heat shock. In cells expressing HDAC6 mutated in the ubiquitin-binding domain, the AAA ATPase factor p97/VCP mediates rapid inactivation of HSF1, precluding late activation of the HSP25 gene. In these cells, knockdown of p97/VCP rescues HSF1 from this rapid inactivation and restores HSP25 expression. We present here a new regulatory circuit that adjusts the duration of the heat shock response to the extent of protein ubiquitination after heat shock. The American Society for Cell Biology 2014-12-15 /pmc/articles/PMC4263459/ /pubmed/25298398 http://dx.doi.org/10.1091/mbc.E14-06-1032 Text en © 2014 Pernet, Faure, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society for Cell Biology. |
spellingShingle | Articles Pernet, Lydia Faure, Virginie Gilquin, Benoit Dufour-Guérin, Solenne Khochbin, Saadi Vourc’h, Claire HDAC6–ubiquitin interaction controls the duration of HSF1 activation after heat shock |
title | HDAC6–ubiquitin interaction controls the duration of HSF1 activation after heat shock |
title_full | HDAC6–ubiquitin interaction controls the duration of HSF1 activation after heat shock |
title_fullStr | HDAC6–ubiquitin interaction controls the duration of HSF1 activation after heat shock |
title_full_unstemmed | HDAC6–ubiquitin interaction controls the duration of HSF1 activation after heat shock |
title_short | HDAC6–ubiquitin interaction controls the duration of HSF1 activation after heat shock |
title_sort | hdac6–ubiquitin interaction controls the duration of hsf1 activation after heat shock |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4263459/ https://www.ncbi.nlm.nih.gov/pubmed/25298398 http://dx.doi.org/10.1091/mbc.E14-06-1032 |
work_keys_str_mv | AT pernetlydia hdac6ubiquitininteractioncontrolsthedurationofhsf1activationafterheatshock AT faurevirginie hdac6ubiquitininteractioncontrolsthedurationofhsf1activationafterheatshock AT gilquinbenoit hdac6ubiquitininteractioncontrolsthedurationofhsf1activationafterheatshock AT dufourguerinsolenne hdac6ubiquitininteractioncontrolsthedurationofhsf1activationafterheatshock AT khochbinsaadi hdac6ubiquitininteractioncontrolsthedurationofhsf1activationafterheatshock AT vourchclaire hdac6ubiquitininteractioncontrolsthedurationofhsf1activationafterheatshock |