Proteostatic

Proteostatic is an adjective relating to proteostasis, the cellular processes that regulate the synthesis, folding, trafficking, and degradation of proteins to maintain a functional proteome. The proteostatic system, or proteostasis network, includes molecular chaperones, the ubiquitin-proteasome system, autophagy-lysosome pathways, and quality-control mechanisms in the endoplasmic reticulum such as ER-associated degradation. Signaling pathways like the heat shock response and the unfolded protein response coordinate the expression and activity of these components in response to stress.

Chaperones assist nascent and misfolded proteins to reach proper conformations and prevent aggregation. The ubiquitin-proteasome system marks damaged or misfolded proteins with ubiquitin for selective degradation. Autophagy targets protein aggregates and damaged organelles for lysosomal breakdown. Together these processes maintain proteome integrity, enable cellular adaptation to stress, and support development and aging.

Proteostatic disruption—due to genetic mutations, environmental stress, aging, or disease—can lead to protein misfolding, aggregation, ER stress, and cellular dysfunction. Accumulating evidence links impaired proteostasis to neurodegenerative diseases such as Alzheimer's, Parkinson's, and Huntington's diseases, as well as metabolic and muscular disorders. Research seeks to understand proteostatic capacity across tissues and organisms and to develop interventions that bolster proteostasis, including chaperone inducers, proteostasis regulators, and enhancers of autophagy or proteasome activity.

Measuring proteostatic capacity relies on stress reporters, biomarkers, and model organisms. The term proteostatic is widely used in cell biology, molecular biology, and aging research to describe processes that maintain the fidelity of the proteome.