Article
An Hsp90 co-chaperone protein in yeast is functionally replaced by site-specific posttranslational modification in humans.
Nature communications - 24 May 2017
Zuehlke Abbey D, Reidy Michael, Lin Coney, LaPointe Paul, Alsomairy Sarah, Lee D Joshua, Rivera-Marquez Genesis M, Beebe Kristin, Prince Thomas, Lee Sunmin, Trepel Jane B, Xu Wanping, Johnson Jill, Masison Daniel, Neckers Len
Abstract excerpt
Heat shock protein 90 (Hsp90) is an essential eukaryotic molecular chaperone. To properly chaperone its clientele, Hsp90 proceeds through an ATP-dependent conformational cycle influenced by posttranslational modifications (PTMs) and assisted by a number of co-chaperone proteins. Although Hsp90 conformational changes in solution have been well-studied, regulation of these complex dynamics in cells remains unclear....
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