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Equilibrium model for hCBS folding in S. cerevisiae. Missense mutant proteins are acted on by two competing systems. If bound by small heat shock proteins, like Hsp26, missense mutant proteins are ubiquitinated and directed to the proteasome for degradation. If bound by Hsp70, mutant proteins are refolded into an active conformation. Proteasome inhibitors alter the equilibrium by both inhibiting the degradation arm, and stimulating the refolding arm by increasing Hsp70 levels.
