Online-Ressource | |
Verfasst von: | Rüthnick, Diana [VerfasserIn] |
Neuner, Annett [VerfasserIn] | |
Dietrich, Franziska [VerfasserIn] | |
Kirrmaier, Daniel [VerfasserIn] | |
Engel, Ulrike [VerfasserIn] | |
Knop, Michael [VerfasserIn] | |
Schiebel, Elmar [VerfasserIn] | |
Titel: | Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes |
Verf.angabe: | Diana Rüthnick, Annett Neuner, Franziska Dietrich, Daniel Kirrmaier, Ulrike Engel, Michael Knop, and Elmar Schiebel |
E-Jahr: | 2017 |
Jahr: | June 28, 2017 |
Umfang: | 18 S. |
Teil: | volume:216 |
year:2017 | |
number:8 | |
pages:2425-2442 | |
extent:18 | |
Fussnoten: | Gesehen am 04.08.2017 |
Titel Quelle: | Enthalten in: The journal of cell biology |
Ort Quelle: | New York, NY : Rockefeller Univ. Press, 1962 |
Jahr Quelle: | 2017 |
Band/Heft Quelle: | 216(2017), 8, Seite 2425-2442 |
ISSN Quelle: | 1540-8140 |
Abstract: | 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. |
DOI: | doi:10.1083/jcb.201612129 |
URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt. Kostenfrei: Volltext ; Verlag: http://dx.doi.org/10.1083/jcb.201612129 |
Kostenfrei: Volltext: http://jcb.rupress.org/content/early/2017/06/27/jcb.201612129 | |
DOI: https://doi.org/10.1083/jcb.201612129 | |
Datenträger: | Online-Ressource |
Sprache: | eng |
K10plus-PPN: | 1561716677 |
Verknüpfungen: | → Zeitschrift |