Status: Bibliographieeintrag
Standort: ---
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| Online-Ressource |
Verfasst von: | Erlemann, Sarah [VerfasserIn]  |
| Neuner, Annett [VerfasserIn]  |
| Gombos, Linda [VerfasserIn]  |
| Schiebel, Elmar [VerfasserIn]  |
Titel: | An extended γ-tubulin ring functions as a stable platform in microtubule nucleation |
Verf.angabe: | Sarah Erlemann, Annett Neuner, Linda Gombos, Romain Gibeaux, Claude Antony, and Elmar Schiebel |
E-Jahr: | 2012 |
Jahr: | 2 April, 2012 |
Umfang: | 16 S. |
Fussnoten: | Gesehen am 22.11.2018 |
Titel Quelle: | Enthalten in: The journal of cell biology |
Ort Quelle: | New York, NY : Rockefeller Univ. Press, 1962 |
Jahr Quelle: | 2012 |
Band/Heft Quelle: | 197(2012), 1, Seite 59-74 |
ISSN Quelle: | 1540-8140 |
Abstract: | Microtubule nucleation sites in yeast consist of a ring of γ-tubulin small complexes and a slight excess of uncomplexed γ-tubulin., γ-Tubulin complexes are essential for microtubule (MT) nucleation. The γ-tubulin small complex (γ-TuSC) consists of two molecules of γ-tubulin and one molecule each of Spc97 and Spc98. In vitro, γ-TuSCs oligomerize into spirals of 13 γ-tubulin molecules per turn. However, the properties and numbers of γ-TuSCs at MT nucleation sites in vivo are unclear. In this paper, we show by fluorescence recovery after photobleaching analysis that γ-tubulin was stably integrated into MT nucleation sites and was further stabilized by tubulin binding. Importantly, tubulin showed a stronger interaction with the nucleation site than with the MT plus end, which probably provides the basis for MT nucleation. Quantitative analysis of γ-TuSCs on single MT minus ends argued for nucleation sites consisting of approximately seven γ-TuSCs with approximately three additional γ-tubulin molecules. Nucleation and anchoring of MTs required the same number of γ-tubulin molecules. We suggest that a spiral of seven γ-TuSCs with a slight surplus of γ-tubulin nucleates MTs in vivo. |
DOI: | doi:10.1083/jcb.201111123 |
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: http://dx.doi.org/10.1083/jcb.201111123 |
| kostenfrei: Volltext: https://rupress.org/jcb/article/197/1/59/36846/An-extended-tubulin-ring-functions-as-a-stable |
| DOI: https://doi.org/10.1083/jcb.201111123 |
Datenträger: | Online-Ressource |
Sprache: | eng |
K10plus-PPN: | 158133429X |
Verknüpfungen: | → Zeitschrift |
¬An¬ extended γ-tubulin ring functions as a stable platform in microtubule nucleation / Erlemann, Sarah [VerfasserIn]; 2 April, 2012 (Online-Ressource)
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