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J Cell Biol. 2016 Dec 19;215(6):823-840. Epub 2016 Dec 5.

MOZART1 and γ-tubulin complex receptors are both required to turn γ-TuSC into an active microtubule nucleation template.

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Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH-Allianz, 69120 Heidelberg, Germany.
Biochemistry Center, 69120 Heidelberg, Germany.
Université Côte d'Azur, Centre National de la Recherche Scientifique, Institut National de la Santé et de la Recherche Médicale, Institut de Biologie Valrose, 06108 Nice, France.
Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH-Allianz, 69120 Heidelberg, Germany


MOZART1/Mzt1 is required for the localization of γ-tubulin complexes to microtubule (MT)-organizing centers from yeast to human cells. Nevertheless, the molecular function of MOZART1/Mzt1 is largely unknown. Taking advantage of the minimal MT nucleation system of Candida albicans, we reconstituted the interactions of Mzt1, γ-tubulin small complex (γ-TuSC), and γ-tubulin complex receptors (γ-TuCRs) Spc72 and Spc110 in vitro. With affinity measurements, domain deletion, and swapping, we show that Spc110 and Mzt1 bind to distinct regions of the γ-TuSC. In contrast, both Mzt1 and γ-TuSC interact with the conserved CM1 motif of Spc110/Spc72. Spc110/Spc72 and Mzt1 constitute "oligomerization chaperones," cooperatively promoting and directing γ-TuSC oligomerization into MT nucleation-competent rings. Consistent with the functions of Mzt1, human MOZART1 directly interacts with the CM1-containing region of the γ-TuCR CEP215. MOZART1 depletion in human cells destabilizes the large γ-tubulin ring complex and abolishes CEP215CM1-induced ectopic MT nucleation. Together, we reveal conserved functions of MOZART1/Mzt1 through interactions with γ-tubulin complex subunits and γ-TuCRs.

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