Molecular cell, 2000-12, Vol.6 (6), p.1355-1364
2000
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- Autor(en) / Beteiligte
- Titel
- ER Stress Induces Cleavage of Membrane-Bound ATF6 by the Same Proteases that Process SREBPs
- Ist Teil von
- Molecular cell, 2000-12, Vol.6 (6), p.1355-1364
- Ort / Verlag
- United States: Elsevier Inc
- Erscheinungsjahr
- 2000
- Quelle
- Free E-Journal (出版社公開部分のみ）
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1097-2765eISSN: 1097-4164DOI: 10.1016/S1097-2765(00)00133-7Titel-ID: cdi_proquest_miscellaneous_72566588
- Format
- –
- Schlagworte
- Activating Transcription Factor 6, Amino Acid Motifs, Amino Acid Sequence, Animals, Carrier Proteins - metabolism, CCAAT-Enhancer-Binding Proteins - metabolism, Cell Line, DNA-Binding Proteins - chemistry, DNA-Binding Proteins - genetics, DNA-Binding Proteins - metabolism, Endopeptidases - genetics, Endopeptidases - metabolism, Endoplasmic Reticulum - metabolism, Heat-Shock Proteins, Humans, Immunoblotting, Intracellular Membranes - metabolism, Intracellular Signaling Peptides and Proteins, Membrane Proteins - chemistry, Membrane Proteins - metabolism, Molecular Chaperones - metabolism, Molecular Sequence Data, Mutation, Proprotein Convertases, Protein Binding, Protein Processing, Post-Translational - drug effects, RNA, Messenger - genetics, RNA, Messenger - metabolism, Sequence Alignment, Serine Endopeptidases - genetics, Serine Endopeptidases - metabolism, Sterol Regulatory Element Binding Protein 1, Thapsigargin - pharmacology, Transcription Factors - chemistry, Transcription Factors - genetics, Transcription Factors - metabolism, Transcription, Genetic - drug effects, Tunicamycin - pharmacology