The unfolded protein response transducer Ire1p contains a nuclear localization sequence recognized by multiple beta importins

Goffin, Laurence, Vodala, Sadanand, Fraser, Christine, Ryan, Joanne, Timms, Mark, Meusburger, Sarina, Catimel, Bruno, Nice, Edouard C., Silver, Pamela A., Xiao, Chong-Yun, Jans, David A. and Gething, Mary-Jane H. (2006) The unfolded protein response transducer Ire1p contains a nuclear localization sequence recognized by multiple beta importins. Molecular biology of the cell, 17 12: 5309-5323. doi:10.1091/mbc.E06-04-0292

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Author Goffin, Laurence
Vodala, Sadanand
Fraser, Christine
Ryan, Joanne
Timms, Mark
Meusburger, Sarina
Catimel, Bruno
Nice, Edouard C.
Silver, Pamela A.
Xiao, Chong-Yun
Jans, David A.
Gething, Mary-Jane H.
Title The unfolded protein response transducer Ire1p contains a nuclear localization sequence recognized by multiple beta importins
Formatted title
The unfolded protein response transducer Ire1p contains a nuclear localization sequence recognized by multiple β importins
Journal name Molecular biology of the cell   Check publisher's open access policy
ISSN 1059-1524
1939-4586
Publication date 2006-12-01
Sub-type Article (original research)
DOI 10.1091/mbc.E06-04-0292
Open Access Status File (Publisher version)
Volume 17
Issue 12
Start page 5309
End page 5323
Total pages 15
Editor David Botstein
Place of publication Bethesda, MD, U.S.A.
Publisher American Society for Cell Biology
Language eng
Subject 0601 Biochemistry and Cell Biology
Formatted 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 α (Kap60p) and a novel βNLS (646KRGSRGGKKGRK657) 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.
© 2006 by The American Society for Cell Biology.

Keyword Ire1p transmembrane receptor kinase/endonuclease
Endoplasmic reticulum (ER)
Saccharomyces cerevisiae
HAC1 mRNA splicing
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
Institute for Molecular Bioscience - Publications
 
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Created: Wed, 24 Mar 2010, 08:44:22 EST by June Temby on behalf of Institute for Molecular Bioscience