TY  - JOUR
AU  - Gunzelmann, Judith
AU  - Rüthnick, Diana
AU  - Lin, Tien-Chen
AU  - Zhang, Wanlu
AU  - Neuner, Annett
AU  - Jäkle, Ursula
AU  - Schiebel, Elmar
TI  - The microtubule polymerase Stu2 promotes oligomerization of the γ-TuSC for cytoplasmic microtubule nucleation.
JO  - eLife
VL  - 7
SN  - 2050-084X
CY  - Cambridge
PB  - eLife Sciences Publications
M1  - DZNE-2020-06550
SP  - e39932
PY  - 2018
AB  - 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.
KW  - Microtubule-Associated Proteins: chemistry
KW  - Microtubule-Associated Proteins: metabolism
KW  - Microtubules: metabolism
KW  - Mutant Proteins: metabolism
KW  - Protein Binding
KW  - Protein Domains
KW  - Protein Multimerization
KW  - Protein Stability
KW  - Saccharomyces cerevisiae Proteins: chemistry
KW  - Saccharomyces cerevisiae Proteins: metabolism
KW  - Tubulin: metabolism
KW  - Microtubule-Associated Proteins (NLM Chemicals)
KW  - Mutant Proteins (NLM Chemicals)
KW  - STU2 protein, S cerevisiae (NLM Chemicals)
KW  - Saccharomyces cerevisiae Proteins (NLM Chemicals)
KW  - Tubulin (NLM Chemicals)
LB  - PUB:(DE-HGF)16
C6  - pmid:30222109
C2  - pmc:PMC6158006
DO  - DOI:10.7554/eLife.39932
UR  - https://pub.dzne.de/record/140228
ER  -