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Significance The protein homeostasis system prevents proteins from misfolding and aggregation. It is unclear, however, how this system is organized to fulfil this role under different insults. To investigate this problem, we examined how six different stresses affected proteome solubility in a mouse neuroblastoma cell line. We found that, although different stresses substantially changed the solubility of many proteins, no proteins substantially aggregated in common. Instead, each stress distinctly remodeled protein–ligand networks involved in key cellular processes, notably SG formation and metabolism. We conclude that cells are endowed with a wide range of regulatory responses, which are tailored for distinct stresses and buffer against widespread protein aggregation.

Widespread remodeling of proteome solubility in response to different protein homeostasis stresses