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- W2116714438 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 642 KKKRKR 647 and/or 653 KKGR 656 ) that is recognized by yeast importin α (Kap60p) and a novel βNLS ( 646 KRGSRGGKKGRK 657 ) that is recognized by several yeast importin β homologues. Kinetic binding data suggest that binding to importin β 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." @default.
- W2116714438 created "2016-06-24" @default.
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- W2116714438 date "2006-12-01" @default.
- W2116714438 modified "2023-09-26" @default.
- W2116714438 title "The Unfolded Protein Response Transducer Ire1p Contains a Nuclear Localization Sequence Recognized by Multiple β Importins" @default.
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- W2116714438 doi "https://doi.org/10.1091/mbc.e06-04-0292" @default.
- W2116714438 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1679693" @default.