Chaperone Biology: stress management

Chaperones are proteins that aid certain proteins, called clients, to attain their functionally correct and right three-dimensional structure. Chaperones work in concert with several proteins called co-chaperones, and together they assist client proteins to load onto and unload from the master chaperone hsp90. Many proteins that depend on hsp90 super chaperone machine for folding happen to be the ones that when mutated or hyper-active cause cancer. In fact many cancers are addicted to these mutated proteins, conferring a survival advantage on cancer over neighboring non-cancerous cells.

Hsp90 super chaperone machine is active overtime in cancer cells. Consequently, inhibition of hsp90 chaperone has been recognized as a strategy to treat cancers, since it results in misfolding and degradation of cancer-causing client proteins. Research efforts at The MCG Cancer Center are focused on elucidating the unique chaperone-client protein biology in the various cancer cell types and developing targeted therapies against the molecular chaperones.

Learn more about the researchers in chaperone biology.

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