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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.

Author information

1
Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH-Allianz, 69120 Heidelberg, Germany.
2
Biochemistry Center, 69120 Heidelberg, Germany.
3
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.
4
Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH-Allianz, 69120 Heidelberg, Germany schiebel.elmar@zmbh.uni-heidelberg.de.

Abstract

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.

PMID:
27920216
PMCID:
PMC5166503
DOI:
10.1083/jcb.201606092
[Indexed for MEDLINE]
Free PMC Article

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