Heat shock response relieves ER stress
In: The EMBO Journal, Jg. 27 (2008-03-06), S. 1049-1059
Online
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Zugriff:
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; ire1Delta 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 ire1Delta 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 that25% 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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Heat shock response relieves ER stress
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Autor/in / Beteiligte Person: | Liu, Yu ; Chang, Amy |
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Zeitschrift: | The EMBO Journal, Jg. 27 (2008-03-06), S. 1049-1059 |
Veröffentlichung: | Wiley, 2008 |
Medientyp: | unknown |
ISSN: | 1460-2075 (print) ; 0261-4189 (print) |
DOI: | 10.1038/emboj.2008.42 |
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