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Conserved function of the HAUS6 calponin homology domain in anchoring augmin for microtubule branching

Augmin is essential for microtubule nucleation during cell division. This study reveals how the conserved calponin homology domain of the augmin subunit HAUS6 binds to microtubules to orient augmin for microtubule branching.

Martin Würtz
Giulia Tonon
Stefan Pfeffer
ResearchOpen Access22 Aug 2025
Nature Communications

Volume: 16, P: 1-20
Structural mechanisms for centrosomal recruitment and organization of the microtubule nucleator γ-TuRC

The γ-TuRC plays a central role for nucleation of microtubules at the centrosome. Here, the authors dissect structural mechanisms for centrosomal recruitment and regulation of the γ-TuRC and identify a role for centriole-lumenal γ-TuRCs.

Qi Gao
Florian W. Hofer
Stefan Pfeffer
ResearchOpen Access12 Mar 2025
Nature Communications

Volume: 16, P: 1-23
Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors

The γ-TuRC plays a key role in regulated nucleation of microtubules (MTs). Here, the authors reveal how yeast γ-TuRC is assembled and activated by dimeric CM1 motifs in receptor protein Spc72 and how MT polymerase Stu2 binds to promote MT assembly.

Anjun Zheng
Bram J. A. Vermeulen
Stefan Pfeffer
ResearchOpen Access05 Jan 2025
Nature Communications

Volume: 16, P: 1-19
An interaction network of inner centriole proteins organised by POC1A-POC1B heterodimer crosslinks ensures centriolar integrity

The inner scaffold is key for centriole stability but its organization is unclear. Here, the authors show the formation of POC1A-POC1B heterodimers, where POC1B resides near the centriole wall and POC1A associates with a POC5 tetramer/Centrin complex.

Cornelia Sala
Martin Würtz
Elmar Schiebel
ResearchOpen Access14 Nov 2024
Nature Communications

Volume: 15, P: 1-20
The augmin complex architecture reveals structural insights into microtubule branching

The formation of branched microtubule networks in mitotic spindles depends on the augmin complex. Zupa, Würtz et al. elucidate the molecular architecture and conformational plasticity of the augmin complex using integrative structural biology, providing structural insights into microtubule branching.

Erik Zupa
Martin Würtz
Stefan Pfeffer
ResearchOpen Access26 Sept 2022
Nature Communications

Volume: 13, P: 1-14
The cryo-EM structure of a γ-TuSC elucidates architecture and regulation of minimal microtubule nucleation systems

The nucleation of microtubules from αβ-tubulin subunits is mediated by γtubulin complexes, which vary in composition across organisms. Here, authors present the cryo-EM structure of the heterotetrameric γ-tubulin small complex (γ-TuSC) from C. albicans at near-atomic resolution.

Erik Zupa
Anjun Zheng
Stefan Pfeffer
ResearchOpen Access11 Nov 2020
Nature Communications

Volume: 11, P: 1-12
CEP44 ensures the formation of bona fide centriole wall, a requirement for the centriole-to-centrosome conversion

During cell division, centrosomes duplicate and newly formed centrioles must undergo centriole-to-centrosome conversion, but the molecular details are unclear. Here, the authors report that the centriole microtubule-triplet 9-fold structure scaffolds pericentriolar proteins and permits the conversion of centrioles to fully functional centrosomes.

Enrico S. Atorino
Shoji Hata
Elmar Schiebel
ResearchOpen Access14 Feb 2020
Nature Communications

Volume: 11, P: 1-15
Modular assembly of the principal microtubule nucleator γ-TuRC

The human microtubule nucleator γ-TuRC is composed of more than thirty subunits, including actin. Here the authors reveal the structural mechanism of modular γ-TuRC assembly and show a functional role of actin in microtubule nucleation.

Martin Würtz
Erik Zupa
Stefan Pfeffer
ResearchOpen Access25 Jan 2022
Nature Communications

Volume: 13, P: 1-16
Insights into the assembly and activation of the microtubule nucleator γ-TuRC

The cryo-EM structure of the γ-tubulin ring complex (γ-TuRC) from Xenopus laevis provides insights into the molecular organization of the complex, and shows that actin is a structural component that is functionally relevant to microtubule nucleation.

Peng Liu
Erik Zupa
Elmar Schiebel
Research19 Dec 2019
Nature

Volume: 578, P: 467-471
GTP regulates the microtubule nucleation activity of γ-tubulin

Schiebel and colleagues use in vitro techniques and yeast genetics to study the role of GTP binding in the microtubule nucleation activity of γ-tubulin.

Linda Gombos
Annett Neuner
Elmar Schiebel
Research27 Oct 2013
Nature Cell Biology

Volume: 15, P: 1317-1327

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