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dc.contributor.author
Pawar, Sumit
dc.contributor.author
Ungricht, Rosemarie
dc.contributor.author
Tiefenboeck, Peter
dc.contributor.author
Leroux, Jean-Christophe
dc.contributor.author
Kutay, Ulrike
dc.date.accessioned
2018-09-10T11:46:07Z
dc.date.available
2017-08-24T08:52:02Z
dc.date.available
2017-08-24T08:59:23Z
dc.date.available
2018-09-10T11:46:07Z
dc.date.issued
2017-08
dc.identifier.other
10.7554/elife.28202
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/180500
dc.identifier.doi
10.3929/ethz-b-000180500
dc.description.abstract
Newly synthesized membrane proteins are targeted to the inner nuclear membrane (INM) by diffusion within the membrane system of the endoplasmic reticulum (ER), translocation through nuclear pore complexes (NPCs) and retention on nuclear partners. Using a visual in vitro assay we previously showed that efficient protein targeting to the INM depends on nucleotide hydrolysis. We now reveal that INM targeting is GTP-dependent. Exploiting in vitro reconstitution and in vivo analysis of INM targeting, we establish that Atlastins, membrane-bound GTPases of the ER, sustain the efficient targeting of proteins to the INM by their continued activity in preserving ER topology. When ER topology is altered, the long-range diffusional exchange of proteins in the ER network and targeting efficiency to the INM are diminished. Highlighting the general importance of proper ER topology, we show that Atlastins also influence NPC biogenesis and timely exit of secretory cargo from the ER.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
eLife Sciences Publications
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.title
Efficient protein targeting to the inner nuclear membrane requires atlastin-dependent maintenance of ER topology
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
dc.date.published
2017
ethz.journal.title
eLife
ethz.journal.volume
6
en_US
ethz.pages.start
e28202
en_US
ethz.size
25 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.identifier.pubmed
28826471
ethz.publication.place
Cambridge
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02517 - Institut für Biochemie / Institute of Biochemistry (IBC)::03543 - Kutay, Ulrike / Kutay, Ulrike
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02020 - Dep. Chemie und Angewandte Biowiss. / Dep. of Chemistry and Applied Biosc.::02534 - Institut für Pharmazeutische Wiss. / Institute of Pharmaceutical Sciences::03811 - Leroux, Jean-Christophe / Leroux, Jean-Christophe
en_US
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02517 - Institut für Biochemie / Institute of Biochemistry (IBC)::03543 - Kutay, Ulrike / Kutay, Ulrike
en_US
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02020 - Dep. Chemie und Angewandte Biowiss. / Dep. of Chemistry and Applied Biosc.::02534 - Institut für Pharmazeutische Wiss. / Institute of Pharmaceutical Sciences::03811 - Leroux, Jean-Christophe / Leroux, Jean-Christophe
ethz.date.deposited
2017-08-24T08:52:03Z
ethz.source
FORM
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2018-09-10T11:46:14Z
ethz.rosetta.lastUpdated
2020-02-15T14:55:20Z
ethz.rosetta.versionExported
true
ethz.COinS
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