An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans

An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans

The eukaryotic heat shock protein 90 (Hsp90) undergoes an ATP-dependent conformational cycle that is influenced by posttranslational modifications and co-chaperones. Here, the authors show that the yeast co-chaperone Hch1 can be functionally substituted by site-specific phosphorylation in human Hsp9...

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Autores principales: Abbey D. Zuehlke, Michael Reidy, Coney Lin, Paul LaPointe, Sarah Alsomairy, D. Joshua Lee, Genesis M. Rivera-Marquez, Kristin Beebe, Thomas Prince, Sunmin Lee, Jane B. Trepel, Wanping Xu, Jill Johnson, Daniel Masison, Len Neckers
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Lenguaje:EN
Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/9b3bc0c73ce4469188b2fc7ff17b707b
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spelling oai:doaj.org-article:9b3bc0c73ce4469188b2fc7ff17b707b2021-12-02T17:06:29ZAn Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans10.1038/ncomms153282041-1723https://doaj.org/article/9b3bc0c73ce4469188b2fc7ff17b707b2017-05-01T00:00:00Zhttps://doi.org/10.1038/ncomms15328https://doaj.org/toc/2041-1723The eukaryotic heat shock protein 90 (Hsp90) undergoes an ATP-dependent conformational cycle that is influenced by posttranslational modifications and co-chaperones. Here, the authors show that the yeast co-chaperone Hch1 can be functionally substituted by site-specific phosphorylation in human Hsp90.Abbey D. ZuehlkeMichael ReidyConey LinPaul LaPointeSarah AlsomairyD. Joshua LeeGenesis M. Rivera-MarquezKristin BeebeThomas PrinceSunmin LeeJane B. TrepelWanping XuJill JohnsonDaniel MasisonLen NeckersNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Abbey D. Zuehlke
Michael Reidy
Coney Lin
Paul LaPointe
Sarah Alsomairy
D. Joshua Lee
Genesis M. Rivera-Marquez
Kristin Beebe
Thomas Prince
Sunmin Lee
Jane B. Trepel
Wanping Xu
Jill Johnson
Daniel Masison
Len Neckers
An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans
description The eukaryotic heat shock protein 90 (Hsp90) undergoes an ATP-dependent conformational cycle that is influenced by posttranslational modifications and co-chaperones. Here, the authors show that the yeast co-chaperone Hch1 can be functionally substituted by site-specific phosphorylation in human Hsp90.
format article
author Abbey D. Zuehlke
Michael Reidy
Coney Lin
Paul LaPointe
Sarah Alsomairy
D. Joshua Lee
Genesis M. Rivera-Marquez
Kristin Beebe
Thomas Prince
Sunmin Lee
Jane B. Trepel
Wanping Xu
Jill Johnson
Daniel Masison
Len Neckers
author_facet Abbey D. Zuehlke
Michael Reidy
Coney Lin
Paul LaPointe
Sarah Alsomairy
D. Joshua Lee
Genesis M. Rivera-Marquez
Kristin Beebe
Thomas Prince
Sunmin Lee
Jane B. Trepel
Wanping Xu
Jill Johnson
Daniel Masison
Len Neckers
author_sort Abbey D. Zuehlke
title An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans
title_short An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans
title_full An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans
title_fullStr An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans
title_full_unstemmed An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans
title_sort hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/9b3bc0c73ce4469188b2fc7ff17b707b
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