![]() ![]() Hence, building capacity to measure proteostasis is important for understanding these maladies as well as understanding more fundamentally how cells manage the foldedness of the proteome under diverse conditions. Proteostasis is also substantially remodelled to support cancer cell survival and changes (possibly detrimentally) upon normal aging. Proteostasis collapse or maladaptation leads to cellular malfunction and is associated with neurodegenerative disease. Quantitatively measuring how well the networks maintaining proteostasis operate remains a nebulous task. In this example, Hsp70 family proteins can target unfolded proteins to foster correct folding and prevent their aggregation. The proteins in this network can engage with different conformations of newly synthesized protein substrate and facilitate the efficiency of the folding reaction. A network of proteins (some key families shown) form a quality control network to manage proteostasis. The net result is “proteostasis” (protein homeostasis), whereby the crowded proteome remains soluble and functional.įigure: Conceptual framework for the biosensor. A key role of these networks is to transiently engage with nascent proteins as they emerge from the ribosome, keep them folded, and degrade them should folding fail or when they reach the end of their natural lifespan. ![]() To govern folding and prevent aggregation, cells employ quality control networks comprising hundreds of proteins. Proteins are particularly prone to misfolding and aggregation relative to other classes of biomolecules because upon synthesis they typically require a complex folding pathway into a unique conformation a process involving the shielding of hydrophobic moieties from aggregation. One of the remarkable features of biology is that a cell can keep its extremely crowded proteome folded and organized without uncontrollable aggregation. ![]()
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