Cancer, heat shock protein 90, and adaptation

I read about this quality of heat shock protein 90 a long time ago and was always puzzled by it because it challenged our conventional view of protein production control.  It means the capacity for adaptation does not require de novo mutations, that the potential for adaptation is often present but suppressed by hsp90, which can let this adaptive potential loose when conditions change or stress occurs. Fascinatingly, hsp90 also binds the key stress receptors, GCs and MRs, and their function requires a dissassociation from the two. So from single cell creatures to us, hsp90 has a strongly conserved evolutionary role, this being rather typical of most heat shock proteins.

Prions and chaperones: Outside the fold

Susan Lindquist has challenged conventional thinking on how misfolded proteins drive disease and may power evolution. But she still finds that criticism stings.