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The augmin complex architecture reveals structural insights into microtubule branching

Author

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  • Erik Zupa

    (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282)

  • Martin Würtz

    (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282)

  • Annett Neuner

    (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282)

  • Thomas Hoffmann

    (European Molecular Biology Laboratory (EMBL), Heidelberg Meyerhofstraße 1)

  • Mandy Rettel

    (European Molecular Biology Laboratory (EMBL), Heidelberg Meyerhofstraße 1)

  • Anna Böhler

    (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282)

  • Bram J. A. Vermeulen

    (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282)

  • Sebastian Eustermann

    (European Molecular Biology Laboratory (EMBL), Heidelberg Meyerhofstraße 1)

  • Elmar Schiebel

    (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282)

  • Stefan Pfeffer

    (Zentrum für Molekulare Biologie der Universität Heidelberg, DKFZ-ZMBH Allianz, Im Neuenheimer Feld 282)

Abstract

In mitosis, the augmin complex binds to spindle microtubules to recruit the γ-tubulin ring complex (γ-TuRC), the principal microtubule nucleator, for the formation of branched microtubules. Our understanding of augmin-mediated microtubule branching is hampered by the lack of structural information on the augmin complex. Here, we elucidate the molecular architecture and conformational plasticity of the augmin complex using an integrative structural biology approach. The elongated structure of the augmin complex is characterised by extensive coiled-coil segments and comprises two structural elements with distinct but complementary functions in γ-TuRC and microtubule binding, linked by a flexible hinge. The augmin complex is recruited to microtubules via a composite microtubule binding site comprising a positively charged unordered extension and two calponin homology domains. Our study provides the structural basis for augmin function in branched microtubule formation, decisively fostering our understanding of spindle formation in mitosis.

Suggested Citation

  • Erik Zupa & Martin Würtz & Annett Neuner & Thomas Hoffmann & Mandy Rettel & Anna Böhler & Bram J. A. Vermeulen & Sebastian Eustermann & Elmar Schiebel & Stefan Pfeffer, 2022. "The augmin complex architecture reveals structural insights into microtubule branching," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-33228-6
    DOI: 10.1038/s41467-022-33228-6
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    References listed on IDEAS

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    1. Justin M. Kollman & Jessica K. Polka & Alex Zelter & Trisha N. Davis & David A. Agard, 2010. "Microtubule nucleating γ-TuSC assembles structures with 13-fold microtubule-like symmetry," Nature, Nature, vol. 466(7308), pages 879-882, August.
    2. Kathryn Tunyasuvunakool & Jonas Adler & Zachary Wu & Tim Green & Michal Zielinski & Augustin Žídek & Alex Bridgland & Andrew Cowie & Clemens Meyer & Agata Laydon & Sameer Velankar & Gerard J. Kleywegt, 2021. "Highly accurate protein structure prediction for the human proteome," Nature, Nature, vol. 596(7873), pages 590-596, August.
    3. Carlos Sánchez-Huertas & Francisco Freixo & Ricardo Viais & Cristina Lacasa & Eduardo Soriano & Jens Lüders, 2016. "Non-centrosomal nucleation mediated by augmin organizes microtubules in post-mitotic neurons and controls axonal microtubule polarity," Nature Communications, Nature, vol. 7(1), pages 1-14, November.
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    Cited by:

    1. Szymon W. Manka, 2023. "Structural insights into how augmin augments the mitotic spindle," Nature Communications, Nature, vol. 14(1), pages 1-3, December.
    2. Sophie M. Travis & Brian P. Mahon & Wei Huang & Meisheng Ma & Michael J. Rale & Jodi Kraus & Derek J. Taylor & Rui Zhang & Sabine Petry, 2023. "Integrated model of the vertebrate augmin complex," Nature Communications, Nature, vol. 14(1), pages 1-10, December.

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