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Reengineering Ribosome Export
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| Zeitschriftentitel: | Molecular Biology of the Cell |
|---|---|
| Personen und Körperschaften: | , |
| In: | Molecular Biology of the Cell, 20, 2009, 5, S. 1545-1554 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
American Society for Cell Biology (ASCB)
|
| Schlagwörter: |
| author_facet |
Lo, Kai-Yin Johnson, Arlen W. Lo, Kai-Yin Johnson, Arlen W. |
|---|---|
| author |
Lo, Kai-Yin Johnson, Arlen W. |
| spellingShingle |
Lo, Kai-Yin Johnson, Arlen W. Molecular Biology of the Cell Reengineering Ribosome Export Cell Biology Molecular Biology |
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lo, kai-yin |
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Lo, Kai-Yin Johnson, Arlen W. 1059-1524 1939-4586 American Society for Cell Biology (ASCB) Cell Biology Molecular Biology http://dx.doi.org/10.1091/mbc.e08-10-1000 <jats:p> Large cargoes require multiple receptors for efficient transport through the nuclear pore complex. The 60S ribosomal subunit is one of the bulkiest transport cargoes, and in yeast three different receptors, Crm1, Mex67/Mtr2, and Arx1, collaborate in its export. However, only Crm1, recruited by the adapter Nmd3, appears to be conserved for 60S export in higher eukaryotes. We asked if export of the large subunit requires specific receptors. We made protein fusions between mutant Nmd3 and various export receptors. Surprisingly, fusions of Mex67, the tRNA exportin Los1, Mtr2, Cse1, or Msn5 to Nmd3, lacking its Crm1-dependent nuclear export signal (NES), all functioned in export. Furthermore, these chimeric proteins supported 60S export even in the presence of the Crm1 inhibitor leptomycin B, indicating that export was now independent of Crm1. These results suggest that there is not a requirement for a specific export receptor for the large subunit, as recruitment of any receptor will suffice. Finally we show that the addition of an NES directly to the 60S ribosomal subunit protein Rpl3 promotes export. These results imply remarkable flexibility in the export pathway for the 60S subunit and help explain how different export receptors could have evolved in different eukaryotic lineages. </jats:p> Reengineering Ribosome Export Molecular Biology of the Cell |
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Molecular Biology of the Cell |
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| title |
Reengineering Ribosome Export |
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Reengineering Ribosome Export |
| title_full |
Reengineering Ribosome Export |
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Reengineering Ribosome Export |
| title_full_unstemmed |
Reengineering Ribosome Export |
| title_short |
Reengineering Ribosome Export |
| title_sort |
reengineering ribosome export |
| topic |
Cell Biology Molecular Biology |
| url |
http://dx.doi.org/10.1091/mbc.e08-10-1000 |
| publishDate |
2009 |
| physical |
1545-1554 |
| description |
<jats:p> Large cargoes require multiple receptors for efficient transport through the nuclear pore complex. The 60S ribosomal subunit is one of the bulkiest transport cargoes, and in yeast three different receptors, Crm1, Mex67/Mtr2, and Arx1, collaborate in its export. However, only Crm1, recruited by the adapter Nmd3, appears to be conserved for 60S export in higher eukaryotes. We asked if export of the large subunit requires specific receptors. We made protein fusions between mutant Nmd3 and various export receptors. Surprisingly, fusions of Mex67, the tRNA exportin Los1, Mtr2, Cse1, or Msn5 to Nmd3, lacking its Crm1-dependent nuclear export signal (NES), all functioned in export. Furthermore, these chimeric proteins supported 60S export even in the presence of the Crm1 inhibitor leptomycin B, indicating that export was now independent of Crm1. These results suggest that there is not a requirement for a specific export receptor for the large subunit, as recruitment of any receptor will suffice. Finally we show that the addition of an NES directly to the 60S ribosomal subunit protein Rpl3 promotes export. These results imply remarkable flexibility in the export pathway for the 60S subunit and help explain how different export receptors could have evolved in different eukaryotic lineages. </jats:p> |
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| author | Lo, Kai-Yin, Johnson, Arlen W. |
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| description | <jats:p> Large cargoes require multiple receptors for efficient transport through the nuclear pore complex. The 60S ribosomal subunit is one of the bulkiest transport cargoes, and in yeast three different receptors, Crm1, Mex67/Mtr2, and Arx1, collaborate in its export. However, only Crm1, recruited by the adapter Nmd3, appears to be conserved for 60S export in higher eukaryotes. We asked if export of the large subunit requires specific receptors. We made protein fusions between mutant Nmd3 and various export receptors. Surprisingly, fusions of Mex67, the tRNA exportin Los1, Mtr2, Cse1, or Msn5 to Nmd3, lacking its Crm1-dependent nuclear export signal (NES), all functioned in export. Furthermore, these chimeric proteins supported 60S export even in the presence of the Crm1 inhibitor leptomycin B, indicating that export was now independent of Crm1. These results suggest that there is not a requirement for a specific export receptor for the large subunit, as recruitment of any receptor will suffice. Finally we show that the addition of an NES directly to the 60S ribosomal subunit protein Rpl3 promotes export. These results imply remarkable flexibility in the export pathway for the 60S subunit and help explain how different export receptors could have evolved in different eukaryotic lineages. </jats:p> |
| doi_str_mv | 10.1091/mbc.e08-10-1000 |
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| imprint | American Society for Cell Biology (ASCB), 2009 |
| imprint_str_mv | American Society for Cell Biology (ASCB), 2009 |
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| language | English |
| last_indexed | 2024-03-01T14:42:58.875Z |
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| physical | 1545-1554 |
| publishDate | 2009 |
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| publisher | American Society for Cell Biology (ASCB) |
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| series | Molecular Biology of the Cell |
| source_id | 49 |
| spelling | Lo, Kai-Yin Johnson, Arlen W. 1059-1524 1939-4586 American Society for Cell Biology (ASCB) Cell Biology Molecular Biology http://dx.doi.org/10.1091/mbc.e08-10-1000 <jats:p> Large cargoes require multiple receptors for efficient transport through the nuclear pore complex. The 60S ribosomal subunit is one of the bulkiest transport cargoes, and in yeast three different receptors, Crm1, Mex67/Mtr2, and Arx1, collaborate in its export. However, only Crm1, recruited by the adapter Nmd3, appears to be conserved for 60S export in higher eukaryotes. We asked if export of the large subunit requires specific receptors. We made protein fusions between mutant Nmd3 and various export receptors. Surprisingly, fusions of Mex67, the tRNA exportin Los1, Mtr2, Cse1, or Msn5 to Nmd3, lacking its Crm1-dependent nuclear export signal (NES), all functioned in export. Furthermore, these chimeric proteins supported 60S export even in the presence of the Crm1 inhibitor leptomycin B, indicating that export was now independent of Crm1. These results suggest that there is not a requirement for a specific export receptor for the large subunit, as recruitment of any receptor will suffice. Finally we show that the addition of an NES directly to the 60S ribosomal subunit protein Rpl3 promotes export. These results imply remarkable flexibility in the export pathway for the 60S subunit and help explain how different export receptors could have evolved in different eukaryotic lineages. </jats:p> Reengineering Ribosome Export Molecular Biology of the Cell |
| spellingShingle | Lo, Kai-Yin, Johnson, Arlen W., Molecular Biology of the Cell, Reengineering Ribosome Export, Cell Biology, Molecular Biology |
| title | Reengineering Ribosome Export |
| title_full | Reengineering Ribosome Export |
| title_fullStr | Reengineering Ribosome Export |
| title_full_unstemmed | Reengineering Ribosome Export |
| title_short | Reengineering Ribosome Export |
| title_sort | reengineering ribosome export |
| title_unstemmed | Reengineering Ribosome Export |
| topic | Cell Biology, Molecular Biology |
| url | http://dx.doi.org/10.1091/mbc.e08-10-1000 |