The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
ER Stress Induces Cleavage of Membrane-Bound ATF6 by the Same Proteases that Process SREBPs
Open accessAbstract
ATF6 is a membrane-bound transcription factor that activates genes in the endoplasmic reticulum (ER) stress response. When unfolded proteins accumulate in the ER, ATF6 is cleaved to release its cytoplasmic domain, which enters the nucleus. Here, we show that ATF6 is processed by Site-1 protease (S1P) and Site-2 protease (S2P), the enzymes that process SREBPs in response to cholesterol deprivation. ATF6 processing was blocked completely in cells lacking S2P and partially in cells lacking S1P. ATF6 processing required the RxxL and asparagine/proline motifs, known requirements for S1P and S2P processing, respectively. Cells lacking S2P failed to induce GRP78, an ATF6 target, in response to ER stress. ATF6 processing did not require SCAP, which is essential for SREBP processing. We conclude that S1P and S2P are required for the ER stress response as well as for lipid synthesis.
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“Accumulation of lipid droplets is a common hallmark of ER stress27,28.”
From APOE4 impairs myelination via cholesterol dysregulation in oligodendrocytes (2022) · cites this paper as [27]
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Cites
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Self-citationAmino Acid Preferences for Specific Locations at the Ends of α Helices
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Regulated Intramembrane Proteolysis
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SREBP-1, a membrane-bound transcription factor released by sterol-regulated proteolysis
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Self-citationActivation of ATF6 and an ATF6 DNA Binding Site by the Endoplasmic Reticulum Stress Response
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Self-citationActivation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response.
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Signal integration in the endoplasmic reticulum unfolded protein response
Ron, D., & Walter, P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2199 · Cited by 6,431
The Unfolded Protein Response: From Stress Pathway to Homeostatic Regulation
Walter, P., & Ron, D. (2011) · Science · doi:10.1126/science.1209038 · Cited by 5,897
Yoshida, H., Matsui, T., Yamamoto, A., Okada, T., & Mori, K. (2001) · Cell · doi:10.1016/s0092-8674(01)00611-0 · Cited by 4,054
THE MAMMALIAN UNFOLDED PROTEIN RESPONSE
Schröder, M., & Kaufman, R. J. (2005) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.73.011303.074134 · Cited by 3,099
Roles of CHOP/GADD153 in endoplasmic reticulum stress
Oyadomari, S., & Mori, M. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401373 · Cited by 2,879
Metadata
- Authors
- Ye, J., Rawson, R. B., Komuro, R., Chen, X., Davé, U. P., Prywes, R., Brown, M. S., & Goldstein, J. L.
- Affiliations
- The University of Texas Southwestern Medical Center (US)
- Columbia University (US)
- Corresponding author
- Brown, Michael S
- Goldstein, Joseph L
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2000-12
- Volume
- 6
- Issue
- 6
- Pages
- 1355-1364
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2127639686
- Cited by
- 1,871
- References
- 27
- Citations by year
- 2026: 60 · 2025: 58 · 2024: 108 · 2023: 98 · 2022: 87 · 2021: 102 · 2020: 93 · 2019: 89 · 2018: 89 · 2017: 69 · 2016: 83 · 2015: 80 · 2014: 58 · 2013: 96 · 2012: 81
- FWCI
- 16.05
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Heart, Lung, and Blood Institute (HL-20948, P01HL020948)
- National Cancer Institute (R01CA050329, CA 50329)
- 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
- ATF6, endoplasmic reticulum stress, site-1 protease, site-2 protease, proteolytic cleavage, GRP78, SCAP, lipogenesis, unfolded protein response
- MeSH terms
- Endoplasmic Reticulum Chaperone BiP, Amino Acid Sequence, Animals, Carrier Proteins, Cell Line, DNA-Binding Proteins, Endoplasmic Reticulum, Heat-Shock Proteins, Humans, Intracellular Membranes, Membrane Proteins, Molecular Sequence Data, Mutation, Endopeptidases, Protein Binding, Protein Processing, Post-Translational, RNA, Messenger, Serine Endopeptidases, Transcription Factors, Transcription, Genetic, Tunicamycin, Immunoblotting, Sequence Alignment, Molecular Chaperones, Thapsigargin, Amino Acid Motifs, CCAAT-Enhancer-Binding Proteins, Proprotein Convertases, Intracellular Signaling Peptides and Proteins, Activating Transcription Factor 6, Sterol Regulatory Element Binding Protein 1
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