Buchumschlag

The microtubule polymerase Stu2 promotes oligomerization of the γ-TuSC for cytoplasmic microtubule nucleation

Stu2/XMAP215/ZYG-9/Dis1/Alp14/Msps/ch-TOG family members in association with with γ-tubulin complexes nucleate microtubules, but we know little about the interplay of these nucleation factors. Here, we show that the budding yeast Stu2 in complex with the γ-tubulin receptor Spc72 nucleates microtubul...

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Hauptverfasser: Gunzelmann, Judith (VerfasserIn) , Rüthnick, Diana (VerfasserIn) , Lin, Dennis Tien-chen (VerfasserIn) , Zhang, Wanlu (VerfasserIn) , Neuner, Annett (VerfasserIn) , Jäkle, Ursula (VerfasserIn) , Schiebel, Elmar (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: September 26, 2018
In: eLife
Year: 2018, Jahrgang: 7
ISSN:2050-084X
DOI:10.7554/eLife.39932
Online-Zugang:Verlag, Volltext: https://doi.org/10.7554/eLife.39932
Volltext
Verfasserangaben:Judith Gunzelmann, Diana Rüthnick, Tien-chen Lin, Wanlu Zhang, Annett Neuner, Ursula Jäkle, Elmar Schiebel
Beschreibung
Zusammenfassung:Stu2/XMAP215/ZYG-9/Dis1/Alp14/Msps/ch-TOG family members in association with with γ-tubulin complexes nucleate microtubules, but we know little about the interplay of these nucleation factors. Here, we show that the budding yeast Stu2 in complex with the γ-tubulin receptor Spc72 nucleates microtubules in vitro without the small γ-tubulin complex (γ-TuSC). Upon γ-TuSC addition, Stu2 facilitates Spc72-γ-TuSC interaction by binding to Spc72 and γ-TuSC. Stu2 together with Spc72-γ-TuSC increases microtubule nucleation in a process that is dependent on the TOG domains of Stu2. Importantly, these activities are also important for microtubule nucleation in vivo. Stu2 stabilizes Spc72-γ-TuSC at the minus end of cytoplasmic microtubules (cMTs) and an in vivo assay indicates that cMT nucleation requires the TOG domains of Stu2. Upon γ-tubulin depletion, we observed efficient cMT nucleation away from the spindle pole body (SPB), which was dependent on Stu2. Thus, γ-TuSC restricts cMT assembly to the SPB whereas Stu2 nucleates cMTs together with γ-TuSC and stabilizes γ-TuSC at the cMT minus end.
Beschreibung:Gesehen am 16.05.2019
Beschreibung:Online Resource
ISSN:2050-084X
DOI:10.7554/eLife.39932

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