Structure, dynamics, evolution, and function of a major scaffold component in the nuclear pore complex
Copyright © 2013 Elsevier Ltd. All rights reserved..
The nuclear pore complex, composed of proteins termed nucleoporins (Nups), is responsible for nucleocytoplasmic transport in eukaryotes. Nuclear pore complexes (NPCs) form an annular structure composed of the nuclear ring, cytoplasmic ring, a membrane ring, and two inner rings. Nup192 is a major component of the NPC's inner ring. We report the crystal structure of Saccharomyces cerevisiae Nup192 residues 2-960 [ScNup192(2-960)], which adopts an α-helical fold with three domains (i.e., D1, D2, and D3). Small angle X-ray scattering and electron microscopy (EM) studies reveal that ScNup192(2-960) could undergo long-range transition between "open" and "closed" conformations. We obtained a structural model of full-length ScNup192 based on EM, the structure of ScNup192(2-960), and homology modeling. Evolutionary analyses using the ScNup192(2-960) structure suggest that NPCs and vesicle-coating complexes are descended from a common membrane-coating ancestral complex. We show that suppression of Nup192 expression leads to compromised nuclear transport and hypothesize a role for Nup192 in modulating the permeability of the NPC central channel.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2013 |
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| Erschienen: |
2013 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:21 |
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| Enthalten in: |
Structure (London, England : 1993) - 21(2013), 4 vom: 02. Apr., Seite 560-71 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Sampathkumar, Parthasarathy [VerfasserIn] |
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| Links: |
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| Themen: |
Journal Article |
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| Anmerkungen: |
Date Completed 30.09.2013 Date Revised 21.10.2021 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.str.2013.02.005 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM225861380 |
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| 100 | 1 | |a Sampathkumar, Parthasarathy |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Structure, dynamics, evolution, and function of a major scaffold component in the nuclear pore complex |
| 264 | 1 | |c 2013 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ƒaComputermedien |b c |2 rdamedia | ||
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| 500 | |a Date Completed 30.09.2013 | ||
| 500 | |a Date Revised 21.10.2021 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2013 Elsevier Ltd. All rights reserved. | ||
| 520 | |a The nuclear pore complex, composed of proteins termed nucleoporins (Nups), is responsible for nucleocytoplasmic transport in eukaryotes. Nuclear pore complexes (NPCs) form an annular structure composed of the nuclear ring, cytoplasmic ring, a membrane ring, and two inner rings. Nup192 is a major component of the NPC's inner ring. We report the crystal structure of Saccharomyces cerevisiae Nup192 residues 2-960 [ScNup192(2-960)], which adopts an α-helical fold with three domains (i.e., D1, D2, and D3). Small angle X-ray scattering and electron microscopy (EM) studies reveal that ScNup192(2-960) could undergo long-range transition between "open" and "closed" conformations. We obtained a structural model of full-length ScNup192 based on EM, the structure of ScNup192(2-960), and homology modeling. Evolutionary analyses using the ScNup192(2-960) structure suggest that NPCs and vesicle-coating complexes are descended from a common membrane-coating ancestral complex. We show that suppression of Nup192 expression leads to compromised nuclear transport and hypothesize a role for Nup192 in modulating the permeability of the NPC central channel | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, N.I.H., Extramural | |
| 650 | 4 | |a Research Support, U.S. Gov't, Non-P.H.S. | |
| 650 | 7 | |a NUP192 protein, S cerevisiae |2 NLM | |
| 650 | 7 | |a Nuclear Pore Complex Proteins |2 NLM | |
| 650 | 7 | |a Saccharomyces cerevisiae Proteins |2 NLM | |
| 700 | 1 | |a Kim, Seung Joong |e verfasserin |4 aut | |
| 700 | 1 | |a Upla, Paula |e verfasserin |4 aut | |
| 700 | 1 | |a Rice, William J |e verfasserin |4 aut | |
| 700 | 1 | |a Phillips, Jeremy |e verfasserin |4 aut | |
| 700 | 1 | |a Timney, Benjamin L |e verfasserin |4 aut | |
| 700 | 1 | |a Pieper, Ursula |e verfasserin |4 aut | |
| 700 | 1 | |a Bonanno, Jeffrey B |e verfasserin |4 aut | |
| 700 | 1 | |a Fernandez-Martinez, Javier |e verfasserin |4 aut | |
| 700 | 1 | |a Hakhverdyan, Zhanna |e verfasserin |4 aut | |
| 700 | 1 | |a Ketaren, Natalia E |e verfasserin |4 aut | |
| 700 | 1 | |a Matsui, Tsutomu |e verfasserin |4 aut | |
| 700 | 1 | |a Weiss, Thomas M |e verfasserin |4 aut | |
| 700 | 1 | |a Stokes, David L |e verfasserin |4 aut | |
| 700 | 1 | |a Sauder, J Michael |e verfasserin |4 aut | |
| 700 | 1 | |a Burley, Stephen K |e verfasserin |4 aut | |
| 700 | 1 | |a Sali, Andrej |e verfasserin |4 aut | |
| 700 | 1 | |a Rout, Michael P |e verfasserin |4 aut | |
| 700 | 1 | |a Almo, Steven C |e verfasserin |4 aut | |
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