Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex
Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs), enormous assemblies composed of multiple copies of ∼30 different proteins called nucleoporins. To unravel the basic scaffold underlying the NPC, we have characterized the species-specific scaffold nucleoporin Nup37 and ELY5/EL...
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| Format: | Article |
| Language: | en_US |
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National Academy of Sciences (U.S.)
2013
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| Online Access: | http://hdl.handle.net/1721.1/76779 https://orcid.org/0000-0001-8012-1512 |
| _version_ | 1826212645472043008 |
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| author | Bilokapic, Silvija Schwartz, Thomas |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Bilokapic, Silvija Schwartz, Thomas |
| author_sort | Bilokapic, Silvija |
| collection | MIT |
| description | Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs), enormous assemblies composed of multiple copies of ∼30 different proteins called nucleoporins. To unravel the basic scaffold underlying the NPC, we have characterized the species-specific scaffold nucleoporin Nup37 and ELY5/ELYS. Both proteins integrate directly via Nup120/160 into the universally conserved heptameric Y-complex, the critical unit for the assembly and functionality of the NPC. We present the crystal structure of Schizosaccharomyces pombe Nup37 in complex with Nup120, a 174-kDa subassembly that forms one of the two short arms of the Y-complex. Nup37 binds near the bend of the L-shaped Nup120 protein, potentially stabilizing the relative orientation of its two domains. By means of reconstitution assays, we pinpoint residues crucial for this interaction. In vivo and in vitro results show that ELY5 binds near an interface of the Nup120–Nup37 complex. Complementary biochemical and cell biological data refine and consolidate the interactions of Nup120 within the current Y-model. Finally, we propose an orientation of the Y-complex relative to the pore membrane, consistent with the lattice model. |
| first_indexed | 2024-09-23T15:32:05Z |
| format | Article |
| id | mit-1721.1/76779 |
| institution | Massachusetts Institute of Technology |
| language | en_US |
| last_indexed | 2024-09-23T15:32:05Z |
| publishDate | 2013 |
| publisher | National Academy of Sciences (U.S.) |
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| spelling | mit-1721.1/767792022-09-29T14:50:55Z Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex Bilokapic, Silvija Schwartz, Thomas Massachusetts Institute of Technology. Department of Biology Schwartz, Thomas Bilokapic, Silvija Nucleocytoplasmic transport is mediated by nuclear pore complexes (NPCs), enormous assemblies composed of multiple copies of ∼30 different proteins called nucleoporins. To unravel the basic scaffold underlying the NPC, we have characterized the species-specific scaffold nucleoporin Nup37 and ELY5/ELYS. Both proteins integrate directly via Nup120/160 into the universally conserved heptameric Y-complex, the critical unit for the assembly and functionality of the NPC. We present the crystal structure of Schizosaccharomyces pombe Nup37 in complex with Nup120, a 174-kDa subassembly that forms one of the two short arms of the Y-complex. Nup37 binds near the bend of the L-shaped Nup120 protein, potentially stabilizing the relative orientation of its two domains. By means of reconstitution assays, we pinpoint residues crucial for this interaction. In vivo and in vitro results show that ELY5 binds near an interface of the Nup120–Nup37 complex. Complementary biochemical and cell biological data refine and consolidate the interactions of Nup120 within the current Y-model. Finally, we propose an orientation of the Y-complex relative to the pore membrane, consistent with the lattice model. National Institutes of Health (U.S.) (Grant GM077537) Pew Charitable Trusts (Pew Scholar Award) Ministry of Science, Education and Sports of the Republic of Croatia (Croatian Science Foundation fellowship) 2013-02-12T17:15:45Z 2013-02-12T17:15:45Z 2012-09 2012-03 Article http://purl.org/eprint/type/JournalArticle 0027-8424 1091-6490 http://hdl.handle.net/1721.1/76779 Bilokapic, S., and T. U. Schwartz. “Molecular Basis for Nup37 and ELY5/ELYS Recruitment to the Nuclear Pore Complex.” Proceedings of the National Academy of Sciences 109.38 (2012): 15241–15246. Web.© 2013 National Academy of Sciences. https://orcid.org/0000-0001-8012-1512 en_US http://dx.doi.org/10.1073/pnas.1205151109 Proceedings of the National Academy of Sciences of the United States of America Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf National Academy of Sciences (U.S.) PNAS |
| spellingShingle | Bilokapic, Silvija Schwartz, Thomas Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex |
| title | Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex |
| title_full | Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex |
| title_fullStr | Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex |
| title_full_unstemmed | Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex |
| title_short | Molecular basis for Nup37 and ELY5/ELYS recruitment to the nuclear pore complex |
| title_sort | molecular basis for nup37 and ely5 elys recruitment to the nuclear pore complex |
| url | http://hdl.handle.net/1721.1/76779 https://orcid.org/0000-0001-8012-1512 |
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