Fig. 1

Molecular mechanisms for proteostasis maintenance Proteostasis can be maintained via three distinct and interlinked mechanisms, including the modulation of protein biogenesis, enhancement of chaperone capacity and prompt clearance of misfolded protein by UPS and autophagy. The ribosomal synthesis of nascent polypeptide is exquisitely modulated. The synthesized polypeptide can be folded into functional proteins with the assistance of chaperones. Chaperones can also function to refold stress-induced misfolded proteins. The misfolded protein can be cleared away by UPS and autophagy. However, the deregulated modulation of protein biogenesis and impairment of chaperone function, UPS and autophagy capacities can lead to disturbed proteostasis and protein aggregate formation