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

Abstract

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.