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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Detalles Bibliográficos
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
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2017
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Science
Q
Acceso en línea:https://doaj.org/article/9b3bc0c73ce4469188b2fc7ff17b707b
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Sumario: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.

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