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dc.contributor.author
Guydosh, Nicholas R.
dc.contributor.author
Kimmig, Philipp
dc.contributor.author
Walter, Peter
dc.contributor.author
Green, Rachel
dc.date.accessioned
2017-12-22T13:09:46Z
dc.date.available
2017-11-22T08:39:48Z
dc.date.available
2017-12-22T13:09:46Z
dc.date.issued
2017
dc.identifier.other
10.7554/eLife.29216
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/211863
dc.identifier.doi
10.3929/ethz-b-000211863
dc.description.abstract
The unfolded protein response (UPR) monitors and adjusts the protein folding capacity of the endoplasmic reticulum (ER). In S. pombe, the ER membrane-resident kinase/endoribonuclease Ire1 utilizes a mechanism of selective degradation of ER-bound mRNAs (RIDD) to maintain homeostasis. We used a genetic screen to identify factors critical to the Ire1-mediated UPR and found several proteins, Dom34, Hbs1 and Ski complex subunits, previously implicated in ribosome rescue and mRNA no-go-decay (NGD). Ribosome profiling in ER-stressed cells lacking these factors revealed that Ire1-mediated cleavage of ER-associated mRNAs results in ribosome stalling and mRNA degradation. Stalled ribosomes iteratively served as a ruler to template precise, regularly spaced upstream mRNA cleavage events. This clear signature uncovered hundreds of novel target mRNAs. Our results reveal that the UPR in S. pombe executes RIDD in an intricate interplay between Ire1, translation, and the NGD pathway, and establish a critical role for NGD in maintaining ER homeostasis.
en_US
dc.language.iso
en
en_US
dc.publisher
eLife Sciences Publ.
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.title
Regulated Ire1-dependent mRNA decay requires no-go mRNA degradation to maintain endoplasmic reticulum homeostasis in S. Pombe
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
dc.date.published
2017-09-25
ethz.journal.title
eLife
ethz.journal.volume
6
en_US
ethz.pages.start
e29216
en_US
ethz.size
20 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
Cambridge
en_US
ethz.publication.status
published
en_US
ethz.date.deposited
2017-11-22T08:39:52Z
ethz.source
SCOPUS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-12-22T13:09:48Z
ethz.rosetta.lastUpdated
2018-11-06T06:05:25Z
ethz.rosetta.versionExported
true
ethz.COinS
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