The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Fine-Tuning of the Unfolded Protein Response: Assembling the IRE1α Interactome
Open accessAbstract
Endoplasmic reticulum (ER) stress is a hallmark feature of secretory cells and many diseases including cancer, neurodegeneration, and diabetes. Adaptation to protein folding stress is mediated by the activation of an integrated signal transduction pathway known as the unfolded protein response (UPR). The UPR signals through three distinct stress sensors located at the ER membrane, IRE1α, ATF6 and PERK. Although PERK and IRE1α share functionally similar ER-luminal sensing domains and both are simultaneously activated in cellular paradigms of ER stress in vitro, they are selectively engaged in vivo by the physiological stress of unfolded proteins. The differences in terms of tissue-specific regulation of the UPR may be explained by the formation of distinct regulatory protein complexes. This concept is supported by the recent identification of adaptor and modulator proteins that directly interact with IRE1α. In this review we discuss recent evidence supporting a model where IRE1α signaling emerges as a highly regulated process, controlled by the formation of a dynamic scaffold onto which many regulatory components assemble.
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Cites
Autophagy in the Pathogenesis of Disease
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Biological and Chemical Approaches to Diseases of Proteostasis Deficiency
Powers, E. T., Morimoto, R. I., Dillin, A., Kelly, J. W., & Balch, W. E. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.052308.114844 · Cited by 1,149
The unfolded protein response signals through high-order assembly of Ire1
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Cited by
Autophagy and the Integrated Stress Response
Kroemer, G., Mariño, G., & Levine, B. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.023 · Cited by 3,506
Mechanisms, regulation and functions of the unfolded protein response
Hetz, C., Zhang, K., & Kaufman, R. J. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0250-z · Cited by 2,666
Self-citationThe Unfolded Protein Response and Cell Fate Control
Hetz, C., & Papa, F. R. (2018) · Molecular Cell · doi:10.1016/j.molcel.2017.06.017 · Cited by 1,544
Self-citationTargeting the unfolded protein response in disease
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Self-citationGetting RIDD of RNA: IRE1 in cell fate regulation
Maurel, M., Chevet, E., Tavernier, J., & Gerlo, S. (2014) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2014.02.008 · Cited by 631
Metadata
- Authors
- Hetz, C., & Glimcher, L. H.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2009-09
- Volume
- 35
- Issue
- 5
- Pages
- 551-561
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2157515789
- Cited by
- 413
- References
- 7
- FWCI
- 14.55
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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