ArticleMolecular biology of the cell2006
The unfolded protein response transducer Ire1p contains a nuclear localization sequence recognized by multiple beta importins.
Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- Exploring the IRE1 interactome: From canonical signaling functions to unexpected roles.The Journal of biological chemistry · 2024Review
- Dissecting the Nuclear Import of the Ribosomal Protein Rps2 (uS5).Biomolecules · 2023Article
- The Sequential Recruitments of Rab-GTPase Ypt1p and the NNS Complex onto pre-Molecular and cellular biology · 2023Article
- DoesMicroorganisms · 2021Article
- Review
- Development of a novel DsRed-NLS vector with a monopartite classical nuclear localization signal.3 Biotech · 2019Article
- Review
- Identification of human short introns.PloS one · 2017Article
- Acute Endoplasmic Reticulum Stress-Independent Unconventional Splicing of XBP1 mRNA in the Nucleus of Mammalian Cells.International journal of molecular sciences · 2015Article
- Article
- Using natural variation in Drosophila to discover previously unknown endoplasmic reticulum stress genes.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Article
- Analysis of prelamin A biogenesis reveals the nucleus to be a CaaX processing compartment.Molecular biology of the cell · 2008Article
- Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins.The Journal of cell biology · 2007Article
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Authors and funding
12 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Ire1p transmembrane receptor kinase/endonuclease transduces the unfolded protein response (UPR) from the endoplasmic reticulum (ER) to the nucleus in Saccharomyces cerevisiae. In this study, we analyzed the capacity of a highly basic sequence in the linker region of Ire1p to function as a nuclear localization sequence (NLS) both in vivo and in vitro. This 18-residue sequence is capable of targeting green fluorescent protein to the nucleus of yeast cells in a process requiring proteins involved in the Ran GTPase cycle that facilitates nuclear import. Mutagenic analysis and importin binding studies demonstrate that the Ire1p linker region contains overlapping potential NLSs: at least one classical NLS (within sequences 642KKKRKR647 and/or 653KKGR656) that is recognized by yeast importin alpha (Kap60p) and a novel betaNLS (646KRGSRGGKKGRK657) that is recognized by several yeast importin beta homologues. Kinetic binding data suggest that binding to importin beta proteins would predominate in vivo. The UPR, and in particular ER stress-induced HAC1 mRNA splicing, is inhibited by point mutations in the Ire1p NLS that inhibit nuclear localization and also requires functional RanGAP and Ran GEF proteins. The NLS-dependent nuclear localization of Ire1p would thus seem to be central to its role in UPR signaling.
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