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Heat shock response relieves ER stress.

The EMBO journal | Apr 9, 2008

http://www.ncbi.nlm.nih.gov/pubmed/18323774

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 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.

Pubmed ID: 18323774 RIS Download

Mesh terms: Biological Transport | COP-Coated Vesicles | Carboxypeptidases | DNA-Binding Proteins | Endoplasmic Reticulum | Genes, Fungal | Golgi Apparatus | Heat-Shock Response | Membrane Glycoproteins | Membrane Proteins | Microbial Viability | Models, Biological | Mutation | Protein Folding | Protein Processing, Post-Translational | Protein-Serine-Threonine Kinases | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Transcription Factors | Vesicular Transport Proteins

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Associated grants

  • Agency: NIGMS NIH HHS, Id: GM 58212

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