Scaffold nucleoporins Nup188 and Nup192 share structural and functional properties with nuclear transport receptors
| Autor: | Andersen, Kasper R., Onischenko, Evgeny, Tang, Jeffrey H, Kumar, Pravin, Chen, James Z., Ulrich, Alexander, Liphardt, Jan T, Weis, Karsten, Schwartz, Thomas |
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| Přispěvatelé: | Massachusetts Institute of Technology. Department of Biology, Andersen, Kasper R., Kumar, Pravin, Chen, James Z., Ulrich, Alexander, Schwartz, Thomas |
| Rok vydání: | 2013 |
| Předmět: |
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Molecular Saccharomyces cerevisiae Proteins QH301-705.5 Science S. cerevisiae Biology macromolecular assemblages General Biochemistry Genetics and Molecular Biology 03 medical and health sciences Structure-Activity Relationship 0302 clinical medicine medicine otorhinolaryngologic diseases Biology (General) Nuclear pore Nuclear export signal Receptor 030304 developmental biology 0303 health sciences nucleocytoplasmic transport General Immunology and Microbiology General Neuroscience General Medicine Cell Biology Biophysics and Structural Biology 3. Good health macromolecular assemblage Nuclear Pore Complex Proteins stomatognathic diseases medicine.anatomical_structure Cytoplasm Nucleocytoplasmic Transport Biophysics Medicine Nucleoporin Nuclear transport Nucleus Myceliophthora thermophila 030217 neurology & neurosurgery Research Article |
| Zdroj: | eLife eLife Sciences Publications, Ltd. eLife, Vol 2 (2013) |
| ISSN: | 2050-084X |
| Popis: | 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) |
| Databáze: | OpenAIRE |
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