Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors
Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs) embedded in the nuclear envelope. About 30 different proteins (nucleoporins, nups) arrange around a central eightfold rotational axis to build the modular NPC. Nup188 and Nup192 are related and evolutionary conserved, large nuc...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | en_US |
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eLife Sciences Publications, Ltd.
2014
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| Online Access: | http://hdl.handle.net/1721.1/89403 https://orcid.org/0000-0001-8012-1512 |
| _version_ | 1811080959060082688 |
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| author | Andersen, Kasper R. Onischenko, Evgeny Tang, Jeffrey H Kumar, Pravin Chen, James Z. Ulrich, Alexander Liphardt, Jan T Weis, Karsten Schwartz, Thomas Andersen, Kasper R. |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Andersen, Kasper R. Onischenko, Evgeny Tang, Jeffrey H Kumar, Pravin Chen, James Z. Ulrich, Alexander Liphardt, Jan T Weis, Karsten Schwartz, Thomas Andersen, Kasper R. |
| author_sort | Andersen, Kasper R. |
| collection | MIT |
| description | Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs) embedded in the nuclear envelope. About 30 different proteins (nucleoporins, nups) arrange around a central eightfold rotational axis to build the modular NPC. Nup188 and Nup192 are related and evolutionary conserved, large nucleoporins that are part of the NPC scaffold. Here we determine the structure of Nup188. The protein folds into an extended stack of helices where an N-terminal 130 kDa segment forms an intricate closed ring, while the C-terminal region is a more regular, superhelical structure. Overall, the structure has distant similarity with flexible S-shaped nuclear transport receptors (NTRs). Intriguingly, like NTRs, both Nup188 and Nup192 specifically bind FG-repeats and are able to translocate through NPCs by facilitated diffusion. This blurs the existing dogma of a clear distinction between stationary nups and soluble NTRs and suggests an evolutionary relationship between the NPC and the soluble nuclear transport machinery. |
| first_indexed | 2024-09-23T11:39:33Z |
| format | Article |
| id | mit-1721.1/89403 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T11:39:33Z |
| publishDate | 2014 |
| publisher | eLife Sciences Publications, Ltd. |
| record_format | dspace |
| spelling | mit-1721.1/894032022-10-01T05:03:44Z Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors Andersen, Kasper R. Onischenko, Evgeny Tang, Jeffrey H Kumar, Pravin Chen, James Z. Ulrich, Alexander Liphardt, Jan T Weis, Karsten Schwartz, Thomas Andersen, Kasper R. Massachusetts Institute of Technology. Department of Biology Andersen, Kasper R. Kumar, Pravin Chen, James Z. Ulrich, Alexander Schwartz, Thomas Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs) embedded in the nuclear envelope. About 30 different proteins (nucleoporins, nups) arrange around a central eightfold rotational axis to build the modular NPC. Nup188 and Nup192 are related and evolutionary conserved, large nucleoporins that are part of the NPC scaffold. Here we determine the structure of Nup188. The protein folds into an extended stack of helices where an N-terminal 130 kDa segment forms an intricate closed ring, while the C-terminal region is a more regular, superhelical structure. Overall, the structure has distant similarity with flexible S-shaped nuclear transport receptors (NTRs). Intriguingly, like NTRs, both Nup188 and Nup192 specifically bind FG-repeats and are able to translocate through NPCs by facilitated diffusion. This blurs the existing dogma of a clear distinction between stationary nups and soluble NTRs and suggests an evolutionary relationship between the NPC and the soluble nuclear transport machinery. National Center for Research Resources (U.S.) (Award RR-15301) National Institutes of Health (U.S.) (R01GM077537) National Institutes of Health (U.S.) (R01GM058065) Lundbeck Foundation Danish Council for Independent Research (DFF Sapere Aude) National Cancer Institute (U.S.) (U54CA143836) 2014-09-09T20:23:07Z 2014-09-09T20:23:07Z 2013-06 2013-03 Article http://purl.org/eprint/type/JournalArticle 2050-084X http://hdl.handle.net/1721.1/89403 Andersen, Kasper R, Evgeny Onischenko, Jeffrey H Tang, Pravin Kumar, James Z Chen, Alexander Ulrich, Jan T Liphardt, Karsten Weis, and Thomas U Schwartz. “Scaffold Nucleoporins Nup188 and Nup192 Share Structural and Functional Properties with Nuclear Transport Receptors.” eLife 2 (June 11, 2013):e00745. https://orcid.org/0000-0001-8012-1512 en_US http://dx.doi.org/10.7554/eLife.00745 eLife Creative Commons Attribution http://creativecommons.org/licenses/by/3.0/ application/pdf eLife Sciences Publications, Ltd. eLife Sciences Publications, Ltd. |
| spellingShingle | Andersen, Kasper R. Onischenko, Evgeny Tang, Jeffrey H Kumar, Pravin Chen, James Z. Ulrich, Alexander Liphardt, Jan T Weis, Karsten Schwartz, Thomas Andersen, Kasper R. Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors |
| title | Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors |
| title_full | Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors |
| title_fullStr | Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors |
| title_full_unstemmed | Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors |
| title_short | Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors |
| title_sort | scaffold nucleoporins nup188 and nup192 share structural and functional properties with nuclear transport receptors |
| url | http://hdl.handle.net/1721.1/89403 https://orcid.org/0000-0001-8012-1512 |
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