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: | English |
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eLife Sciences Publications Ltd
2013-06-01
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| Series: | eLife |
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| Online Access: | https://elifesciences.org/articles/00745 |
| _version_ | 1811236941983645696 |
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| author | Kasper R Andersen Evgeny Onischenko Jeffrey H Tang Pravin Kumar James Z Chen Alexander Ulrich Jan T Liphardt Karsten Weis Thomas U Schwartz |
| author_facet | Kasper R Andersen Evgeny Onischenko Jeffrey H Tang Pravin Kumar James Z Chen Alexander Ulrich Jan T Liphardt Karsten Weis Thomas U Schwartz |
| author_sort | Kasper R Andersen |
| collection | DOAJ |
| 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 | 2024-04-12T12:16:45Z |
| format | Article |
| id | doaj.art-6669b1c42e1f479ca7e21b29abb64729 |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T12:16:45Z |
| publishDate | 2013-06-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-6669b1c42e1f479ca7e21b29abb647292022-12-22T03:33:24ZengeLife Sciences Publications LtdeLife2050-084X2013-06-01210.7554/eLife.00745Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptorsKasper R Andersen0Evgeny Onischenko1Jeffrey H Tang2Pravin Kumar3James Z Chen4Alexander Ulrich5Jan T Liphardt6Karsten Weis7Thomas U Schwartz8Department of Biology, Massachusetts Institute of Technology, Cambridge, United StatesDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United StatesDepartment of Physics, University of California, Berkeley, Berkeley, United StatesDepartment of Biology, Massachusetts Institute of Technology, Cambridge, United StatesDepartment of Biology, Massachusetts Institute of Technology, Cambridge, United StatesDepartment of Biology, Massachusetts Institute of Technology, Cambridge, United StatesDepartment of Physics, University of California, Berkeley, Berkeley, United StatesDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, United StatesDepartment of Biology, Massachusetts Institute of Technology, Cambridge, United StatesNucleocytoplasmic 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.https://elifesciences.org/articles/00745nucleocytoplasmic transportmacromolecular assemblageMyceliophthora thermophila |
| spellingShingle | Kasper R Andersen Evgeny Onischenko Jeffrey H Tang Pravin Kumar James Z Chen Alexander Ulrich Jan T Liphardt Karsten Weis Thomas U Schwartz Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors eLife nucleocytoplasmic transport macromolecular assemblage Myceliophthora thermophila |
| 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 |
| topic | nucleocytoplasmic transport macromolecular assemblage Myceliophthora thermophila |
| url | https://elifesciences.org/articles/00745 |
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