FIGURE 1: Hch1 interaction to yeast Hsp90 and phosphorylation of Y627 in human Hsp90 impact client chaperoning through restricting Hsp90 conformational changes. (A) Normal ATP-driven client chaperoning in both humans and yeast. Appropriate interaction of Hsp90 with Hch1 (yeast) or phosphorylation of Hsp90-Y627 (human) promotes release of chaperoned client. (B) Deregulated Hch1 interaction with yeast Hsp90 restricts its conformational flexibility, resulting in reduced client chaperoning. (C) Deregulated phosphorylation of human Hsp90 at Y627 phenocopies consequences of deregulated Hch1 interaction in yeast.

By continuing to use the site, you agree to the use of cookies. more information

The cookie settings on this website are set to "allow cookies" to give you the best browsing experience possible. If you continue to use this website without changing your cookie settings or you click "Accept" below then you are consenting to this. Please refer to our "privacy statement" and our "terms of use" for further information.