%0 Journal Article
%A Gunzelmann, Judith
%A Rüthnick, Diana
%A Lin, Tien-Chen
%A Zhang, Wanlu
%A Neuner, Annett
%A Jäkle, Ursula
%A Schiebel, Elmar
%T The microtubule polymerase Stu2 promotes oligomerization of the γ-TuSC for cytoplasmic microtubule nucleation.
%J eLife
%V 7
%@ 2050-084X
%C Cambridge
%I eLife Sciences Publications
%M DZNE-2020-06550
%P e39932
%D 2018
%X 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.
%K Microtubule-Associated Proteins: chemistry
%K Microtubule-Associated Proteins: metabolism
%K Microtubules: metabolism
%K Mutant Proteins: metabolism
%K Protein Binding
%K Protein Domains
%K Protein Multimerization
%K Protein Stability
%K Saccharomyces cerevisiae Proteins: chemistry
%K Saccharomyces cerevisiae Proteins: metabolism
%K Tubulin: metabolism
%K Microtubule-Associated Proteins (NLM Chemicals)
%K Mutant Proteins (NLM Chemicals)
%K STU2 protein, S cerevisiae (NLM Chemicals)
%K Saccharomyces cerevisiae Proteins (NLM Chemicals)
%K Tubulin (NLM Chemicals)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:30222109
%2 pmc:PMC6158006
%R 10.7554/eLife.39932
%U https://pub.dzne.de/record/140228