Home > Publications Database > The microtubule polymerase Stu2 promotes oligomerization of the γ-TuSC for cytoplasmic microtubule nucleation. > print

001     140228
005     20240504120055.0
024 7 _ |a 10.7554/eLife.39932
|2 doi
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037 _ _ |a DZNE-2020-06550
041 _ _ |a English
082 _ _ |a 600
100 1 _ |a Gunzelmann, Judith
|0 P:(DE-HGF)0
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245 _ _ |a The microtubule polymerase Stu2 promotes oligomerization of the γ-TuSC for cytoplasmic microtubule nucleation.
260 _ _ |a Cambridge
|c 2018
|b eLife Sciences Publications
264 _ 1 |3 online
|2 Crossref
|b eLife Sciences Publications, Ltd
|c 2018-09-17
336 7 _ |a article
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336 7 _ |a Output Types/Journal article
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336 7 _ |a ARTICLE
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336 7 _ |a Journal Article
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520 _ _ |a 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.
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542 _ _ |i 2018-09-17
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|u http://creativecommons.org/licenses/by/4.0/
588 _ _ |a Dataset connected to CrossRef, PubMed,
650 _ 7 |a Microtubule-Associated Proteins
|2 NLM Chemicals
650 _ 7 |a Mutant Proteins
|2 NLM Chemicals
650 _ 7 |a STU2 protein, S cerevisiae
|2 NLM Chemicals
650 _ 7 |a Saccharomyces cerevisiae Proteins
|2 NLM Chemicals
650 _ 7 |a Tubulin
|2 NLM Chemicals
650 _ 2 |a Microtubule-Associated Proteins: chemistry
|2 MeSH
650 _ 2 |a Microtubule-Associated Proteins: metabolism
|2 MeSH
650 _ 2 |a Microtubules: metabolism
|2 MeSH
650 _ 2 |a Mutant Proteins: metabolism
|2 MeSH
650 _ 2 |a Protein Binding
|2 MeSH
650 _ 2 |a Protein Domains
|2 MeSH
650 _ 2 |a Protein Multimerization
|2 MeSH
650 _ 2 |a Protein Stability
|2 MeSH
650 _ 2 |a Saccharomyces cerevisiae Proteins: chemistry
|2 MeSH
650 _ 2 |a Saccharomyces cerevisiae Proteins: metabolism
|2 MeSH
650 _ 2 |a Tubulin: metabolism
|2 MeSH
700 1 _ |a Rüthnick, Diana
|0 P:(DE-HGF)0
|b 1
700 1 _ |a Lin, Tien-Chen
|0 P:(DE-2719)2812342
|b 2
|u dzne
700 1 _ |a Zhang, Wanlu
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700 1 _ |a Neuner, Annett
|0 P:(DE-HGF)0
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700 1 _ |a Jäkle, Ursula
|0 P:(DE-HGF)0
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700 1 _ |a Schiebel, Elmar
|0 P:(DE-HGF)0
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|e Corresponding author
773 1 8 |a 10.7554/elife.39932
|b : eLife Sciences Publications, Ltd, 2018-09-17
|3 journal-article
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|t eLife
|v 7
|y 2018
|x 2050-084X
773 _ _ |a 10.7554/eLife.39932
|g Vol. 7, p. e39932
|0 PERI:(DE-600)2687154-3
|q 7|p e39932
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|v 7
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856 4 _ |y OpenAccess
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856 4 _ |y OpenAccess
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856 7 _ |2 Pubmed Central
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