Eukaryotic proteins that are no longer needed or are misfolded or otherwise damaged are usually marked for destruction by the polyubiquitation pathway. These ubiquitinated proteins are recognized and degraded by the 26S proteasome. Hence the 26S proteasome is an integral part of the cell's mechanism to degrade proteins. Furthermore, a constant supply of functional Hsp90 is needed to maintain the tertiary structure of the proteasome. Finally experiments done with heat sensitive Hsp90 mutants and the 26S proteasome suggest that Hsp90 is responsible for most, if not all, of the ATPase activity of the proteasome.