Heat shock protein (HSP90)
belongs to a family of molecular chaperones which are rapid and
abundantly induced by stresses. HSP90 plays a crucial role in
stabilizing denatured proteins that have become misfolded or
unfolded because of cellular stress and by aiding in their
re-folding. So far, many of the proteins identified as HSP90
clients are key components of the oncogenic phenotype involved in
controlling many of the hallmarks of cancer.
Inhibiting Hsp90 has the potential to affect all the hallmarks
of cancer, making it an exciting potential therapeutic target.
HSP90 inhibitors that bind the ATP binding pocket standing on the
N-terminal of HSP90 have resulted in degradation of HSP90 client
proteins through the ubiquitin proteasome pathway. The natural
product of HSP90 inhibitors geldanamycin and radicicol can exert
their antitumor function by blocking the intrinsic ATPase activity
of HSP90, leading to degradation of HSP90 client proteins. Thus,
HSP90 inhibition provides an important pharmacological platform for
anticancer therapy.
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