Proteome solubility is differentially reshaped by thermal stress and regulators of ubiquitination.

ABSTRACT: The ubiquitin-proteasome system maintains proteostasis by degrading proteins that unfold and become insoluble upon stress. Some proteins have high insolubility in normal conditions because of their structure, subcellular localization, and interactions but it remains incompletely understood how the ubiquitin-proteasome system regulates them. Here, we utilized mass spectrometry to profile heat-induced solubility changes (insolubilome) and associated post-translational modifications in human cells (http://thermal-stress-insolubilome.stjude.org). We find that the solubility of several protein categories is oppositely modulated by thermal stress. Some proteins become more soluble upon heat shock, whereas others, including several ubiquitin-conjugating enzymes, become more insoluble. By analyzin

SUBMITTER: Hunt LC 

PROVIDER: S-EPMC12391699 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature