Ceapins block the unfolded protein response sensor ATF6α by inducing a neomorphic inter-organelle tether
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The unfolded protein response (UPR) detects and restores deficits in the endoplasmic reticulum (ER) protein folding capacity. Ceapins specifically inhibit the UPR sensor ATF6α, an ER-tethered transcription factor, by retaining it at the ER through an unknown mechanism. Our genome-wide CRISPR interference (CRISPRi) screen reveals that Ceapins function is completely dependent on the ABCD3 peroxisomal transporter. Proteomics studies establish that ABCD3 physically associates with ER-resident ATF6α in cells and in vitro in a Ceapin-dependent manner. Ceapins induce the neomorphic association of ER and peroxisomes by directly tethering the cytosolic domain of ATF6α to ABCD3’s transmembrane regions without inhibiting or depending on ABCD3 transporter activity. Thus, our studies reveal that Ceapins function by chemical-induced misdirection which explains their remarkable specificity and opens up new mechanistic routes for drug development and synthetic biology.
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Ceapin-A7 induces neomorphic association of ATF6a in the endoplasmic reticulum with ABCD3 in the peroxisome, acting as an inter-organelle glue.
“Ceapin-A7 induces the neomorphic association of ATF6a in the endoplasmic reticulum with ABCD3 in the peroxisome, hence acting as an inter-organelle glue.114”
From Chasing molecular glue degraders: screening approaches (2022) · cites this paper as [114]
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- Authors
- Torres, S. E., Gallagher, C. M., Plate, L., Gupta, M., Liem, C. R., Guo, X., Tian, R., Stroud, R. M., Kampmann, M., Weissman, J. S., & Walter, P.
- Affiliations
- Howard Hughes Medical Institute (US)
- Vanderbilt University (US)
- University of California, San Francisco (US)
- Corresponding author
- Weissman, Jonathan S
- Walter, Peter
- ORCID
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2019-05-31
- Volume
- 8
- ISSN
- 2050-084X (ISSN-L)
- PMC
- PMC6588346
- OpenAlex
- W2947250947
- Cited by
- 76
- References
- 41
- Citations by year
- 2026: 12 · 2025: 12 · 2024: 9 · 2023: 8 · 2022: 10 · 2021: 15 · 2020: 8 · 2019: 2
- FWCI
- 4.63
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- eLife (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- eScholarship (California Digital Library) (submittedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institutes of Health (GM111126, DP2 OD021007)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Keywords
- unfolded protein response, ATF6α, ABCD3, endoplasmic reticulum, peroxisomes
- MeSH terms
- Endoplasmic Reticulum, Humans, Phenotype, Protein Binding, Organelles, ATP-Binding Cassette Transporters, Peroxisomes, Activating Transcription Factor 6, Small Molecule Libraries, Unfolded Protein Response, Hep G2 Cells, HEK293 Cells, CRISPR-Cas Systems
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