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A short linear motif in scaffold Nup145C connects Y-complex with pre-assembled outer ring Nup82 complex

The Nup82-Nup159-Nsp1 complex, which plays a key role in mRNA export, is recruited late during the process of nuclear pore complex (NPC) assembly. Here the authors combine crosslinking mass spectrometry, biochemical reconstitution and molecular modeling to gain insights into the mechanism of Nup82 r...

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Bibliographische Detailangaben
Hauptverfasser: Teimer, Roman (VerfasserIn) , Kosinski, Jan (VerfasserIn) , Appen, Alexander von (VerfasserIn) , Beck, Martin (VerfasserIn) , Hurt, Ed (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 24 October 2017
In: Nature Communications
Year: 2017, Jahrgang: 8
ISSN:2041-1723
DOI:10.1038/s41467-017-01160-9
Online-Zugang:Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1038/s41467-017-01160-9
Verlag, kostenfrei, Volltext: https://www.nature.com/articles/s41467-017-01160-9
Volltext
Verfasserangaben:Roman Teimer, Jan Kosinski, Alexander von Appen, Martin Beck & Ed Hurt
Beschreibung
Zusammenfassung:The Nup82-Nup159-Nsp1 complex, which plays a key role in mRNA export, is recruited late during the process of nuclear pore complex (NPC) assembly. Here the authors combine crosslinking mass spectrometry, biochemical reconstitution and molecular modeling to gain insights into the mechanism of Nup82 recruitment to the NPC.
Beschreibung:Gesehen am 21.07.2020
Beschreibung:Online Resource
ISSN:2041-1723
DOI:10.1038/s41467-017-01160-9

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