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Heat shock response relieves ER stress.

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

Authors

  • Liu Y
  • Chang A

Journal

The EMBO journal

Publication Data

April 9, 2008

Associated Grants

  • Agency: NIGMS NIH HHS, Id: GM 58212

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