Cited by 1,871Endoplasmic Reticulum Stress and DiseaseIon Channels and ReceptorsCellular transport and secretion

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ER Stress Induces Cleavage of Membrane-Bound ATF6 by the Same Proteases that Process SREBPs

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Ye, Jin, Rawson, Robert B, Komuro, Ryutaro, Chen, Xi, Davé, Utpal P, Prywes, Ron, Brown, Michael S, Goldstein, Joseph L·2000·Molecular Cell

DOI 10.1016/s1097-2765(00)00133-7

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Abstract

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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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
ORCID: Ye, Jin
Chen, Xi
Davé, Utpal P
Prywes, Ron
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)
DOI: 10.1016/s1097-2765(00)00133-7
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: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 4611 d)
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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ER Stress Induces Cleavage of Membrane-Bound ATF6 by the Same Proteases that Process SREBPs

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