Protein Quality Control is the essential, integrated cellular network of surveillance and repair mechanisms responsible for ensuring that all proteins are correctly folded, functional, and present in the appropriate concentration. This system actively monitors the proteome, identifying and either refolding misfolded proteins using chaperones or targeting irreparably damaged proteins for degradation via the ubiquitin-proteasome system or autophagy. Maintaining robust control is vital for preventing the accumulation of toxic protein aggregates.
Origin
This concept is foundational to molecular cell biology and biochemistry, acknowledging that protein integrity is paramount for all life processes. The system evolved to manage the inherent instability of proteins under cellular stress. In the context of aging and hormonal health, the decline of this control system is a major driver of cellular senescence and age-related pathology.
Mechanism
The process is managed by a suite of heat shock proteins (HSPs) and other chaperones that assist in folding newly synthesized proteins and refolding damaged ones. If refolding fails, the protein is tagged with ubiquitin, signaling the proteasome for destruction. Hormones, particularly thyroid and growth hormones, can modulate the expression and activity of these quality control components, linking endocrine status directly to cellular proteostasis and longevity.
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