Skip to main page content
U.S. flag
See More

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 2002 Dec;10(6):1307-18.
doi: 10.1016/s1097-2765(02)00785-2.

Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

Barry Panaretou  1 , Giuliano Siligardi, Philippe Meyer, Alison Maloney, Janis K Sullivan, Shradha Singh, Stefan H Millson, Paul A Clarke, Soren Naaby-Hansen, Rob Stein, Rainer Cramer, Mehdi Mollapour, Paul Workman, Peter W Piper, Laurence H Pearl, Chrisostomos Prodromou
Affiliations
Free article

Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1

Barry Panaretou et al. Mol Cell. 2002 Dec.
Free article

Abstract

Client protein activation by Hsp90 involves a plethora of cochaperones whose roles are poorly defined. A ubiquitous family of stress-regulated proteins have been identified (Aha1, activator of Hsp90 ATPase) that bind directly to Hsp90 and are required for the in vivo Hsp90-dependent activation of clients such as v-Src, implicating them as cochaperones of the Hsp90 system. In vitro, Aha1 and its shorter homolog, Hch1, stimulate the inherent ATPase activity of yeast and human Hsp90. The identification of these Hsp90 cochaperone activators adds to the complex roles of cochaperones in regulating the ATPase-coupled conformational changes of the Hsp90 chaperone cycle.

PubMed Disclaimer

Comment in

Publication types

MeSH terms

Substances