Regulation of the unfolded protein response in yeast by oxidative stress
| Autor: | John Hanna, Angel Guerra-Moreno, Hendrik Welsch, Marco Jochem, Jessie Ang |
|---|---|
| Rok vydání: | 2019 |
| Předmět: |
Saccharomyces cerevisiae Proteins
Biophysics Saccharomyces cerevisiae Protein Serine-Threonine Kinases medicine.disease_cause Biochemistry Article 03 medical and health sciences Structural Biology Transcription (biology) Gene Expression Regulation Fungal Genetics medicine Cysteine Molecular Biology Gene Caenorhabditis elegans 030304 developmental biology 0303 health sciences Membrane Glycoproteins biology Chemistry 030302 biochemistry & molecular biology Cell Biology biology.organism_classification Hedgehog signaling pathway Yeast Cell biology Repressor Proteins Oxidative Stress Basic-Leucine Zipper Transcription Factors Unfolded Protein Response Unfolded protein response Oxidative stress Signal Transduction |
| Zdroj: | FEBS Lett |
| ISSN: | 1873-3468 0014-5793 |
| DOI: | 10.1002/1873-3468.13389 |
| Popis: | In the unfolded protein response (UPR), Ire1 activates Hac1 to coordinate the transcription of hundreds of genes to mitigate ER stress. Recent work in Caenorhabditis elegans suggests that oxidative stress inhibits this canonical Ire1 signalling pathway, activating instead an antioxidant stress response. We sought to determine whether this novel mode of UPR function also existed in yeast, where Ire1 has been best characterized. We show that the yeast UPR is also subject to inhibition by oxidative stress. Inhibition is mediated by a single evolutionarily conserved cysteine, and affects both luminal and membrane pathways of Ire1 activation. In yeast, Ire1 appears dispensable for resistance to oxidative stress and, therefore, the physiological significance of this pathway remains to be demonstrated. |
| Databáze: | OpenAIRE |
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