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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| Main Authors: | , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
24 October 2017
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| In: |
Nature Communications
Year: 2017, Volume: 8 |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-017-01160-9 |
| Online Access: | 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 
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| Author Notes: | Roman Teimer, Jan Kosinski, Alexander von Appen, Martin Beck & Ed Hurt |
| Summary: | 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. |
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| Item Description: | Gesehen am 21.07.2020 |
| Physical Description: | Online Resource |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-017-01160-9 |