期刊
EMBO JOURNAL
卷 27, 期 7, 页码 1049-1059出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/emboj.2008.42
关键词
ER stress; heat shock response; unfolded protein response; vesicle transport
资金
- NIGMS NIH HHS [R01 GM058212, GM 58212] Funding Source: Medline
Accumulation of misfolded protein in the endoplasmic reticulum (ER) causes stress. The unfolded protein response (UPR), a transcriptional induction pathway, is activated to relieve ER stress. Although UPR is not essential for viability, UPR-deficient cells are more sensitive to ER stress; ire1 Delta cells cannot grow when challenged with tunicamycin or by overexpression of misfolded CPY*. In these cells, multiple functions are defective, including translocation, ER-associated degradation (ERAD), and ER-to-Golgi transport. We tested whether heat shock response (HSR) can relieve ER stress. Using a constitutively active Hsf1 transcription factor to induce HSR without temperature shift, we find that HSR rescues growth of stressed ire1D cells, and partially relieves defects in translocation and ERAD. Cargo-specific effects of constitutively active Hsf1 on ER-to-Golgi transport are correlated with enhanced protein levels of the respective cargo receptors. In vivo, HSR is activated by ER stress, albeit to a lower level than that caused by heat. Genomic analysis of HSR targets reveals that >25% have function in common with UPR targets. We propose that HSR can relieve stress in UPR-deficient cells by affecting multiple ER activities.
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