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@ARTICLE{Gunzelmann:140228,
      author       = {Gunzelmann, Judith and Rüthnick, Diana and Lin, Tien-Chen
                      and Zhang, Wanlu and Neuner, Annett and Jäkle, Ursula and
                      Schiebel, Elmar},
      title        = {{T}he microtubule polymerase {S}tu2 promotes
                      oligomerization of the γ-{T}u{SC} for cytoplasmic
                      microtubule nucleation.},
      journal      = {eLife},
      volume       = {7},
      issn         = {2050-084X},
      address      = {Cambridge},
      publisher    = {eLife Sciences Publications},
      reportid     = {DZNE-2020-06550},
      pages        = {e39932},
      year         = {2018},
      abstract     = {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.},
      keywords     = {Microtubule-Associated Proteins: chemistry /
                      Microtubule-Associated Proteins: metabolism / Microtubules:
                      metabolism / Mutant Proteins: metabolism / Protein Binding /
                      Protein Domains / Protein Multimerization / Protein
                      Stability / Saccharomyces cerevisiae Proteins: chemistry /
                      Saccharomyces cerevisiae Proteins: metabolism / Tubulin:
                      metabolism / Microtubule-Associated Proteins (NLM Chemicals)
                      / Mutant Proteins (NLM Chemicals) / STU2 protein, S
                      cerevisiae (NLM Chemicals) / Saccharomyces cerevisiae
                      Proteins (NLM Chemicals) / Tubulin (NLM Chemicals)},
      cin          = {AG Bradke},
      ddc          = {600},
      cid          = {I:(DE-2719)1013002},
      pnm          = {341 - Molecular Signaling (POF3-341)},
      pid          = {G:(DE-HGF)POF3-341},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30222109},
      pmc          = {pmc:PMC6158006},
      doi          = {10.7554/eLife.39932},
      url          = {https://pub.dzne.de/record/140228},
}