Co-chaperone proteins are important mediators of protein triage, deciding whether misfolded proteins should be degraded or refolded. The accumulation of misfolded proteins is thought to be a major contributing factor to polyglutamine diseases, where the expansion of a polyglutamine tract in the disease protein leads to a conformational change in the protein's structure. A major consequence of this misfolding is the formation of intracellular inclusions, which are thought to play an important role in disease pathogenesis.