期刊
JOURNAL OF PROTEOME RESEARCH
卷 21, 期 5, 页码 1251-1261出版社
AMER CHEMICAL SOC
DOI: 10.1021/acs.jproteome.1c00920
关键词
heat shock; chaperone; recovery; protein solubility; heat shock protein 70; disaggregation; quantitative proteomics
资金
- National Health and Medical Research Council [APP1161803]
- Australian Research Council [DP170103093]
During the recovery from heat shock, eukaryotic cells rapidly down-regulate prefoldins and translation machinery, while mobilizing protein quality control mechanisms, changing cellular energy metabolism, translational activity, and actin cytoskeleton. Long-term adaptation to stress involves the renewal of core cellular components.
Eukaryotic cells respond to heat shock through several regulatory processes including upregulation of stress responsive chaperones and reversible shutdown of cellular activities through formation of protein assemblies. However, the underlying regulatory mechanisms of the recovery of these heat-induced protein assemblies remain largely elusive. Here, we measured the proteome abundance and solubility changes during recovery from heat shock in the mouse Neuro2a cell line. We found that prefoldins and translation machinery are rapidly down-regulated as the first step in the heat shock response. Analysis of proteome solubility reveals that a rapid mobilization of protein quality control machineries, along with changes in cellular energy metabolism, translational activity, and actin cytoskeleton are fundamental to the early stress responses. In contrast, longer term adaptation to stress involves renew al of core cellular components. Inhibition of the Hsp70 family, pivotal for the heat shock response, selectively and negatively affects the ribosomal machinery and delays the solubility recovery of many nuclear proteins. ProteomeXchange: PXD030069.
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