Interactions of the proteasomal system with chaperones: protein triage and protein quality control.

摘要: Unfolded, misfolded, or modified proteins are able to induce proteotoxic cell stress. To prevent stress, it is crucial have a functional protein quality control system, especially in the cytosol and endoplasmic reticulum where newly synthesized. The leading actors this system ubiquitin-proteasomal huge family of heat shock chaperones. Both systems interact with each other, influencing decision whether becomes (re)folded degraded. Especially upon cellular such as oxidative drastically upregulated, supporting, regulating proteasomal degradation defect proteins. Failure one can be compensated partially by upregulation other. Nevertheless, prolonged failure proteasome chaperones results aggregation dysfunction.