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Modular assembly of the principal microtubule nucleator γ-TuRC

Author

Listed:
  • Martin Würtz

    (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz)

  • Erik Zupa

    (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz)

  • Enrico S. Atorino

    (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz)

  • Annett Neuner

    (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz)

  • Anna Böhler

    (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz)

  • Ariani S. Rahadian

    (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz)

  • Bram J. A. Vermeulen

    (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz)

  • Giulia Tonon

    (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz)

  • Sebastian Eustermann

    (European Molecular Biology Laboratory (EMBL))

  • Elmar Schiebel

    (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz)

  • Stefan Pfeffer

    (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz)

Abstract

The gamma-tubulin ring complex (γ-TuRC) is the principal microtubule nucleation template in vertebrates. Recent cryo-EM reconstructions visualized the intricate quaternary structure of the γ-TuRC, containing more than thirty subunits, raising fundamental questions about γ-TuRC assembly and the role of actin as an integral part of the complex. Here, we reveal the structural mechanism underlying modular γ-TuRC assembly and identify a functional role of actin in microtubule nucleation. During γ-TuRC assembly, a GCP6-stabilized core comprising GCP2-3-4-5-4-6 is expanded by stepwise recruitment, selective stabilization and conformational locking of four pre-formed GCP2-GCP3 units. Formation of the lumenal bridge specifies incorporation of the terminal GCP2-GCP3 unit and thereby leads to closure of the γ-TuRC ring in a left-handed spiral configuration. Actin incorporation into the complex is not relevant for γ-TuRC assembly and structural integrity, but determines γ-TuRC geometry and is required for efficient microtubule nucleation and mitotic chromosome alignment in vivo.

Suggested Citation

  • Martin Würtz & Erik Zupa & Enrico S. Atorino & Annett Neuner & Anna Böhler & Ariani S. Rahadian & Bram J. A. Vermeulen & Giulia Tonon & Sebastian Eustermann & Elmar Schiebel & Stefan Pfeffer, 2022. "Modular assembly of the principal microtubule nucleator γ-TuRC," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-28079-0
    DOI: 10.1038/s41467-022-28079-0
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    Cited by:

    1. Anjun Zheng & Bram J. A. Vermeulen & Martin Würtz & Annett Neuner & Nicole Lübbehusen & Matthias P. Mayer & Elmar Schiebel & Stefan Pfeffer, 2025. "Structural insights into the interplay between microtubule polymerases, γ-tubulin complexes and their receptors," Nature Communications, Nature, vol. 16(1), pages 1-19, December.

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