The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
IRE1 and efferent signaling from the endoplasmic reticulum
Abstract
Genetic analysis of the cellular adaptation to malfolded proteins in the endoplasmic reticulum (the unfolded protein response – UPR) has revealed a novel signaling pathway initiated by activation of IRE1, an ER-resident protein kinase and endonuclease. In yeast, Ire1p activates gene expression by promoting a non-conventional splicing event that converts the mRNA encoding the Hac1p transcription factor from an inefficiently translated inactive mRNA to an actively translated one. Hac1p binds to the promoters of genes encoding chaperones and other targets of the UPR and activates them. Recently, mammalian IRE1 homologues have been identified and their response to ER stress is regulated by binding to the ER chaperone BiP. The mechanisms by which mammalian IRE1 activates gene expression have not been completely characterized and mammalian HAC1 homologues have not been identified. Surprisingly, mammalian IRE1s are able to activate both JUN N-terminal kinases and an alternative ER-stress signaling pathway mediated by the transcription factor ATF6. This indicates that the mammalian UPR is more complex than that found in yeast.
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Citations
Cites
Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase
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Self-citationDynamic interaction of BiP and ER stress transducers in the unfolded-protein response
Bertolotti, A., Zhang, Y., Hendershot, L. M., Harding, H. P., & Ron, D. (2000) · Nature Cell Biology · doi:10.1038/35014014 · Cited by 2,860
Self-citationKaufman, R. J. (1999) · Genes & Development · doi:10.1101/gad.13.10.1211 · Cited by 2,248
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Regulated Intramembrane Proteolysis
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Cited by
Orchestrating the unfolded protein response in health and disease
Kaufman, R. J. (2002) · Journal of Clinical Investigation · doi:10.1172/jci0216886 · Cited by 1,015
Franceschi, C., Garagnani, P., Vitale, G., Capri, M., & Salvioli, S. (2017) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2016.09.005 · Cited by 997
Iwakoshi, N. N., Lee, A.-H., Vallabhajosyula, P., Otipoby, K. L., Rajewsky, K., & Glimcher, L. H. (2003) · Nature Immunology · doi:10.1038/ni907 · Cited by 880
Proteasome inhibitors disrupt the unfolded protein response in myeloma cells
Lee, A.-H., Iwakoshi, N. N., Anderson, K. C., & Glimcher, L. H. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1334037100 · Cited by 601
OKADA, T., YOSHIDA, H., AKAZAWA, R., NEGISHI, M., & MORI, K. (2002) · Biochemical Journal · doi:10.1042/bj20020391 · Cited by 522
Metadata
- Authors
- Urano, F., Bertolotti, A., & Ron, D.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2000-11-01
- Volume
- 113
- Issue
- 21
- Pages
- 3697-3702
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W1930219409
- Cited by
- 270
- References
- 42
- FWCI
- 6.65
- Type
- journal article
- Language
- en
- Open access
- closed
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