Mitochondrial stress is relayed to the cytosol by an OMA1–DELE1–HRI pathway
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Abstract
In mammalian cells, mitochondrial dysfunction triggers the integrated stress response, in which the phosphorylation of eukaryotic translation initiation factor 2α (eIF2α) results in the induction of the transcription factor ATF4 1-3. However, how mitochondrial stress is relayed to ATF4 is unknown. Here we show that HRI is the eIF2α kinase that is necessary and sufficient for this relay. In a genome-wide CRISPR interference screen, we identified factors upstream of HRI: OMA1, a mitochondrial stress-activated protease; and DELE1, a little-characterized protein that we found was associated with the inner mitochondrial membrane. Mitochondrial stress stimulates OMA1-dependent cleavage of DELE1 and leads to the accumulation of DELE1 in the cytosol, where it interacts with HRI and activates the eIF2α kinase activity of HRI. In addition, DELE1 is required for ATF4 translation downstream of eIF2α phosphorylation. Blockade of the OMA1-DELE1-HRI pathway triggers an alternative response in which specific molecular chaperones are induced. The OMA1-DELE1-HRI pathway therefore represents a potential therapeutic target that could enable fine-tuning of the integrated stress response for beneficial outcomes in diseases that involve mitochondrial dysfunction.
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ACSL4 enriches cellular membranes with long PUFAs and is required for ferroptosis.
“ACSL4, encoding Acyl-CoA Synthetase Long Chain Family Member 4, which enriches cellular membranes with long PUFAs is required for ferroptosis44,45.”
From Genome-wide CRISPRi/a screens in human neurons link lysosomal failure to ferroptosis (2021) · cites this paper as [45]
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- Authors
- Guo, X., Aviles, G., Liu, Y., Tian, R., Unger, B. A., Lin, Y.-H. T., Wiita, A. P., Xu, K., Correia, M. A., & Kampmann, M.
- Affiliations
- University of California, San Francisco (US)
- Chan Zuckerberg Biohub San Francisco (US)
- Corresponding author
- Kampmann, Martin
- ORCID
- Venue
- Nature
- Published
- 2020-03-04
- Volume
- 579
- Issue
- 7799
- Pages
- 427-432
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- PMC
- PMC7147832
- OpenAlex
- W3010473434
- Cited by
- 674
- References
- 63
- Citations by year
- 2026: 127 · 2025: 121 · 2024: 124 · 2023: 97 · 2022: 93 · 2021: 69 · 2020: 38 · 2019: 4
- FWCI
- 37.00
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Nature (publishedVersion)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- National Institutes of Health (1s10od010786-01, OD022552, DK26506)
- National Institute of General Medical Sciences (DP2GM123500, R01GM044037, DP2GM119139)
- National Institute of Diabetes and Digestive and Kidney Diseases (R56DK026506, R01DK026506)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- mitochondrial stress, integrated stress response, OMA1, human-robot interaction, eIF2α kinase, eIF2α phosphorylation, ATF4, mitochondrial protease, mitochondrial dysfunction, molecular chaperones, inner mitochondrial membrane, therapeutic target
- MeSH terms
- Cell Line, Cytosol, Enzyme Activation, Humans, Male, Metalloendopeptidases, Mitochondria, Phosphorylation, Protein Binding, Stress, Physiological, Eukaryotic Initiation Factor-2, Molecular Chaperones, eIF-2 Kinase, Mitochondrial Proteins, Activating Transcription Factor 4, CRISPR-Cas Systems
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