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Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes
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| Veröffentlicht in: | The journal of cell biology 216(2017), 8, Seite 2425-2442 |
|---|---|
| Personen und Körperschaften: | , , , , , , |
| Titel: | Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes/ Diana Rüthnick, Annett Neuner, Franziska Dietrich, Daniel Kirrmaier, Ulrike Engel, Michael Knop, and Elmar Schiebel |
| Format: | E-Book-Kapitel |
| Sprache: | Englisch |
| veröffentlicht: |
June 28, 2017
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| Gesamtaufnahme: |
: The journal of cell biology, 216(2017), 8, Seite 2425-2442
, volume:216 |
| Quelle: | Verbunddaten SWB Lizenzfreie Online-Ressourcen |
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| 245 | 1 | 0 | |a Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes |c Diana Rüthnick, Annett Neuner, Franziska Dietrich, Daniel Kirrmaier, Ulrike Engel, Michael Knop, and Elmar Schiebel |
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| 520 | |a The spindle pole body (SPB) of budding yeast duplicates once per cell cycle. In G1, the satellite, an SPB precursor, assembles next to the mother SPB (mSPB) on the cytoplasmic side of the nuclear envelope (NE). How the growing satellite subsequently inserts into the NE is an open question. To address this, we have uncoupled satellite growth from NE insertion. We show that the bridge structure that separates the mSPB from the satellite is a distance holder that prevents deleterious fusion of both structures. Binding of the γ-tubulin receptor Spc110 to the central plaque from within the nucleus is important for NE insertion of the new SPB. Moreover, we provide evidence that a nuclear pore complex associates with the duplicating SPB and helps to insert the SPB into the NE. After SPB insertion, membrane-associated proteins including the conserved Ndc1 encircle the SPB and retain it within the NE. Thus, uncoupling SPB growth from NE insertion unmasks functions of the duplication machinery. | ||
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| author | Rüthnick, Diana, Neuner, Annett, Dietrich, Franziska, Kirrmaier, Daniel, Engel, Ulrike, Knop, Michael, Schiebel, Elmar |
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| contents | The spindle pole body (SPB) of budding yeast duplicates once per cell cycle. In G1, the satellite, an SPB precursor, assembles next to the mother SPB (mSPB) on the cytoplasmic side of the nuclear envelope (NE). How the growing satellite subsequently inserts into the NE is an open question. To address this, we have uncoupled satellite growth from NE insertion. We show that the bridge structure that separates the mSPB from the satellite is a distance holder that prevents deleterious fusion of both structures. Binding of the γ-tubulin receptor Spc110 to the central plaque from within the nucleus is important for NE insertion of the new SPB. Moreover, we provide evidence that a nuclear pore complex associates with the duplicating SPB and helps to insert the SPB into the NE. After SPB insertion, membrane-associated proteins including the conserved Ndc1 encircle the SPB and retain it within the NE. Thus, uncoupling SPB growth from NE insertion unmasks functions of the duplication machinery. |
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| spelling | Rüthnick, Diana 1986- VerfasserIn (DE-588)1131566351 (DE-627)886148545 (DE-576)488295866 aut, Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes Diana Rüthnick, Annett Neuner, Franziska Dietrich, Daniel Kirrmaier, Ulrike Engel, Michael Knop, and Elmar Schiebel, June 28, 2017, 18, Text txt rdacontent, Computermedien c rdamedia, Online-Ressource cr rdacarrier, Gesehen am 04.08.2017, The spindle pole body (SPB) of budding yeast duplicates once per cell cycle. In G1, the satellite, an SPB precursor, assembles next to the mother SPB (mSPB) on the cytoplasmic side of the nuclear envelope (NE). How the growing satellite subsequently inserts into the NE is an open question. To address this, we have uncoupled satellite growth from NE insertion. We show that the bridge structure that separates the mSPB from the satellite is a distance holder that prevents deleterious fusion of both structures. Binding of the γ-tubulin receptor Spc110 to the central plaque from within the nucleus is important for NE insertion of the new SPB. Moreover, we provide evidence that a nuclear pore complex associates with the duplicating SPB and helps to insert the SPB into the NE. After SPB insertion, membrane-associated proteins including the conserved Ndc1 encircle the SPB and retain it within the NE. Thus, uncoupling SPB growth from NE insertion unmasks functions of the duplication machinery., Neuner, Annett 1970- VerfasserIn (DE-588)130046256 (DE-627)488789702 (DE-576)297967452 aut, Dietrich, Franziska 1989- VerfasserIn (DE-588)1137713356 (DE-627)895076829 (DE-576)491716826 aut, Kirrmaier, Daniel VerfasserIn (DE-588)1064187080 (DE-627)813075866 (DE-576)423831496 aut, Engel, Ulrike VerfasserIn (DE-588)1123163480 (DE-627)879999721 (DE-576)48164525X aut, Knop, Michael VerfasserIn (DE-588)1064187552 (DE-627)813076749 (DE-576)423832107 aut, Schiebel, Elmar 1960- VerfasserIn (DE-588)1034622595 (DE-627)746029462 (DE-576)165868597 aut, Enthalten in The journal of cell biology New York, NY : Rockefeller Univ. Press, 1962 216(2017), 8, Seite 2425-2442 Online-Ressource (DE-627)242065244 (DE-600)1421310-2 (DE-576)065026527 1540-8140 nnns, volume:216 year:2017 number:8 pages:2425-2442 extent:18, http://dx.doi.org/10.1083/jcb.201612129 Verlag Resolving-System kostenfrei Volltext, http://jcb.rupress.org/content/early/2017/06/27/jcb.201612129 Verlag kostenfrei Volltext, http://dx.doi.org/10.1083/jcb.201612129 LFER, LFER 2017-08-09T00:00:00Z |
| spellingShingle | Rüthnick, Diana, Neuner, Annett, Dietrich, Franziska, Kirrmaier, Daniel, Engel, Ulrike, Knop, Michael, Schiebel, Elmar, Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes, The spindle pole body (SPB) of budding yeast duplicates once per cell cycle. In G1, the satellite, an SPB precursor, assembles next to the mother SPB (mSPB) on the cytoplasmic side of the nuclear envelope (NE). How the growing satellite subsequently inserts into the NE is an open question. To address this, we have uncoupled satellite growth from NE insertion. We show that the bridge structure that separates the mSPB from the satellite is a distance holder that prevents deleterious fusion of both structures. Binding of the γ-tubulin receptor Spc110 to the central plaque from within the nucleus is important for NE insertion of the new SPB. Moreover, we provide evidence that a nuclear pore complex associates with the duplicating SPB and helps to insert the SPB into the NE. After SPB insertion, membrane-associated proteins including the conserved Ndc1 encircle the SPB and retain it within the NE. Thus, uncoupling SPB growth from NE insertion unmasks functions of the duplication machinery. |
| swb_id_str | 491716672 |
| title | Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes |
| title_auth | Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes |
| title_full | Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes Diana Rüthnick, Annett Neuner, Franziska Dietrich, Daniel Kirrmaier, Ulrike Engel, Michael Knop, and Elmar Schiebel |
| title_fullStr | Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes Diana Rüthnick, Annett Neuner, Franziska Dietrich, Daniel Kirrmaier, Ulrike Engel, Michael Knop, and Elmar Schiebel |
| title_full_unstemmed | Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes Diana Rüthnick, Annett Neuner, Franziska Dietrich, Daniel Kirrmaier, Ulrike Engel, Michael Knop, and Elmar Schiebel |
| title_in_hierarchy | Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes / Diana Rüthnick, Annett Neuner, Franziska Dietrich, Daniel Kirrmaier, Ulrike Engel, Michael Knop, and Elmar Schiebel, |
| title_short | Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes |
| title_sort | characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes |
| url | http://dx.doi.org/10.1083/jcb.201612129, http://jcb.rupress.org/content/early/2017/06/27/jcb.201612129 |