Chen, S., Novick, P. & Ferro-Novick, S. ER structure and function. Curr. Opin. Cell Biol. 25, 428–433 (2013).
Article CAS PubMed PubMed Central Google Scholar
Walter, P. & Ron, D. The unfolded protein response: from stress pathway to homeostatic regulation. Science 334, 1081–1086 (2011).
Article CAS PubMed Google Scholar
Hetz, C., Zhang, K. & Kaufman, R. J. Mechanisms, regulation and functions of the unfolded protein response. Nat. Rev. Mol. Cell Biol. 21, 421–438 (2020).
Article CAS PubMed PubMed Central Google Scholar
Mori, K., Ma, W., Gething, M. J. & Sambrook, J. A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus. Cell 74, 743–756 (1993).
Article CAS PubMed Google Scholar
Cox, J. S., Shamu, C. E. & Walter, P. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 73, 1197–1206 (1993).
Article CAS PubMed Google Scholar
Tirasophon, W., Welihinda, A. A. & Kaufman, R. J. A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells. Genes Dev. 12, 1812–1824 (1998).
Article CAS PubMed PubMed Central Google Scholar
Sidrauski, C. & Walter, P. The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response. Cell 90, 1031–1039 (1997).
Article CAS PubMed Google Scholar
Shamu, C. E. & Walter, P. Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus. EMBO J. 15, 3028–3039 (1996).
Article CAS PubMed PubMed Central Google Scholar
Welihinda, A. A. & Kaufman, R. J. The unfolded protein response pathway in Saccharomyces cerevisiae. Oligomerization and trans-phosphorylation of Ire1p (Ern1p) are required for kinase activation. J. Biol. Chem. 271, 18181–18187 (1996).
Article CAS PubMed Google Scholar
Maurel, M., Chevet, E., Tavernier, J. & Gerlo, S. Getting RIDD of RNA: IRE1 in cell fate regulation. Trends Biochem. Sci. 39, 245–254 (2014).
Article CAS PubMed Google Scholar
Hollien, J. & Weissman, J. S. Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response. Science 313, 104–107 (2006).
Article CAS PubMed Google Scholar
Lu, Y., Liang, F. X. & Wang, X. A synthetic biology approach identifies the mammalian UPR RNA ligase RtcB. Mol. Cell 55, 758–770 (2014).
Article PubMed PubMed Central Google Scholar
Hetz, C., Martinon, F., Rodriguez, D. & Glimcher, L. H. The unfolded protein response: integrating stress signals through the stress sensor IRE1alpha. Physiol. Rev. 91, 1219–1243 (2011).
Article CAS PubMed Google Scholar
Hetz, C. The unfolded protein response: controlling cell fate decisions under ER stress and beyond. Nat. Rev. Mol. Cell Biol. 13, 89–102 (2012).
Article CAS PubMed Google Scholar
Hetz, C., Chevet, E. & Oakes, S. A. Proteostasis control by the unfolded protein response. Nat. Cell Biol. 17, 829–838 (2015).
Article CAS PubMed PubMed Central Google Scholar
Bettigole, S. E. & Glimcher, L. H. Endoplasmic reticulum stress in immunity. Annu. Rev. Immunol. 33, 107–138 (2015).
Article CAS PubMed Google Scholar
Huang, S., Xing, Y. & Liu, Y. Emerging roles for the ER stress sensor IRE1α in metabolic regulation and disease. J. Biol. Chem. 294, 18726–18741 (2019).
Article CAS PubMed PubMed Central Google Scholar
Chen, X. & Cubillos-Ruiz, J. R. Endoplasmic reticulum stress signals in the tumour and its microenvironment. Nat. Rev. Cancer 21, 71–88 (2021).
Article CAS PubMed Google Scholar
Kimata, Y. et al. Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins. J. Cell Biol. 179, 75–86 (2007).
Article CAS PubMed PubMed Central Google Scholar
Li, H., Korennykh, A. V., Behrman, S. L. & Walter, P. Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering. Proc. Natl Acad. Sci. USA 107, 16113–16118 (2010).
Article CAS PubMed PubMed Central Google Scholar
Belyy, V., Tran, N. H. & Walter, P. Quantitative microscopy reveals dynamics and fate of clustered IRE1alpha. Proc. Natl Acad. Sci. USA 117, 1533–1542 (2020).
Article CAS PubMed Google Scholar
Ricci, D. et al. Clustering of IRE1α depends on sensing ER stress but not on its RNase activity. FASEB J. 33, 9811–9827 (2019).
Article CAS PubMed PubMed Central Google Scholar
Belyy, V., Zuazo-Gaztelu, I., Alamban, A., Ashkenazi, A. & Walter, P. Endoplasmic reticulum stress activates human IRE1α through reversible assembly of inactive dimers into small oligomers. Elife 11, e74342 (2022).
Article CAS PubMed PubMed Central Google Scholar
Alberti, S. & Hyman, A. A. Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing. Nat. Rev. Mol. Cell Biol. 22, 196–213 (2021).
Article CAS PubMed Google Scholar
Banani, S. F., Lee, H. O., Hyman, A. A. & Rosen, M. K. Biomolecular condensates: organizers of cellular biochemistry. Nat. Rev. Mol. Cell Biol. 18, 285–298 (2017).
Article CAS PubMed PubMed Central Google Scholar
Shin, Y. & Brangwynne, C. P. Liquid phase condensation in cell physiology and disease. Science 357, eaaf4382 (2017).
Lyon, A. S., Peeples, W. B. & Rosen, M. K. A framework for understanding the functions of biomolecular condensates across scales. Nat. Rev. Mol. Cell Biol. 22, 215–235 (2021).
Article CAS PubMed Google Scholar
Hirose, T., Ninomiya, K., Nakagawa, S. & Yamazaki, T. A guide to membraneless organelles and their various roles in gene regulation. Nat. Rev. Mol. Cell Biol. 24, 288–304 (2022).
Protter, D. S. W. & Parker, R. Principles and properties of stress granules. Trends Cell Biol. 26, 668–679 (2016).
Article CAS PubMed PubMed Central Google Scholar
Panas, M. D., Ivanov, P. & Anderson, P. Mechanistic insights into mammalian stress granule dynamics. J. Cell Biol. 215, 313–323 (2016).
Article CAS PubMed PubMed Central Google Scholar
Namkoong, S., Ho, A., Woo, Y. M., Kwak, H. & Lee, J. H. Systematic characterization of stress-induced RNA granulation. Mol. Cell 70, 175–187 e178 (2018).
Article CAS PubMed PubMed Central Google Scholar
Markmiller, S. et al. Context-dependent and disease-specific diversity in protein interactions within stress granules. Cell 172, 590–604 e513 (2018).
Article CAS PubMed PubMed Central Google Scholar
Tourriere, H. et al. The RasGAP-associated endoribonuclease G3BP mediates stress granule assembly. J. Cell Biol. 222 e200212128072023new. (2023)
Gilks, N. et al. Stress granule assembly is mediated by prion-like aggregation of TIA-1. Mol. Biol. Cell 15, 5383–5398 (2004).
Article CAS PubMed PubMed Central Google Scholar
Jain, S. et al. ATPase-modulated stress granules contain a diverse proteome and substructure. Cell 164, 487–498 (2016).
Article CAS PubMed PubMed Central Google Scholar
Yang, P. et al. G3BP1 is a tunable switch that triggers phase separation to assemble stress granules. Cell 181, 325–345 e328 (2020).
Article CAS PubMed PubMed Central Google Scholar
Sanders, D. W. et al. Competing protein–RNA Interaction networks control multiphase intracellular organization. Cell 181, 306–324 e328 (2020).
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