Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors

Anjun Zheng, Bram J. A. Vermeulen, Martin Würtz, Annett Neuner, Nicole Lübbehusen, Matthias P. Mayer, Elmar Schiebel () and Stefan Pfeffer ()
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Anjun Zheng: Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH)
Bram J. A. Vermeulen: Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH)
Martin Würtz: Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH)
Annett Neuner: Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH)
Nicole Lübbehusen: Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH)
Matthias P. Mayer: Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH)
Elmar Schiebel: Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH)
Stefan Pfeffer: Zentrum für Molekulare Biologie der Universität Heidelberg (ZMBH)

Nature Communications, 2025, vol. 16, issue 1, 1-19

Abstract: Abstract The γ-tubulin ring complex (γ-TuRC) is a structural template for controlled nucleation of microtubules from α/β-tubulin heterodimers. At the cytoplasmic side of the yeast spindle pole body, the CM1-containing receptor protein Spc72 promotes γ-TuRC assembly from seven γ-tubulin small complexes (γ-TuSCs) and recruits the microtubule polymerase Stu2, yet their molecular interplay remains unclear. Here, we determine the cryo-EM structure of the Candida albicans cytoplasmic nucleation unit at 3.6 Å resolution, revealing how the γ-TuRC is assembled and conformationally primed for microtubule nucleation by the dimerised Spc72 CM1 motif. Two coiled-coil regions of Spc72 interact with the conserved C-terminal α-helix of Stu2 and thereby position the α/β-tubulin-binding TOG domains of Stu2 in the vicinity of the microtubule assembly site. Collectively, we reveal the function of CM1 motifs in γ-TuSC oligomerisation and the recruitment of microtubule polymerases to the γ-TuRC.

Date: 2025
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DOI: 10.1038/s41467-024-55778-7

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