Journal Article

DZNE-2020-06550

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png The microtubule polymerase Stu2 promotes oligomerization of the γ-TuSC for cytoplasmic microtubule nucleation.

Gunzelmann, J. ; Rüthnick, D. ; Lin, T.-C.DZNE* ; Zhang, W. ; Neuner, A. ; Jäkle, U. ; Schiebel, E. (Corresponding author)

2018
eLife Sciences Publications Cambridge

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Please use a persistent id in citations: doi:10.7554/eLife.39932

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.

Keyword(s): Microtubule-Associated Proteins: chemistry (MeSH) ; Microtubule-Associated Proteins: metabolism (MeSH) ; Microtubules: metabolism (MeSH) ; Mutant Proteins: metabolism (MeSH) ; Protein Binding (MeSH) ; Protein Domains (MeSH) ; Protein Multimerization (MeSH) ; Protein Stability (MeSH) ; Saccharomyces cerevisiae Proteins: chemistry (MeSH) ; Saccharomyces cerevisiae Proteins: metabolism (MeSH) ; Tubulin: metabolism (MeSH) ; Microtubule-Associated Proteins ; Mutant Proteins ; STU2 protein, S cerevisiae ; Saccharomyces cerevisiae Proteins ; Tubulin

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Contributing Institute(s):

1. Axon Growth and Regeneration (AG Bradke)

Research Program(s):

1. 341 - Molecular Signaling (POF3-341) (POF3-341)

Appears in the scientific report 2018

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