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The companion of cellulose synthase 1 confers salt tolerance through a Tau-like mechanism in plants

Author

Listed:
  • Christopher Kesten

    (ETH Zurich
    University of Melbourne
    Max-Planck-Institute of Molecular Plant Physiology)

  • Arndt Wallmann

    (Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), NMR-supported Structural Biology)

  • René Schneider

    (University of Melbourne
    Max-Planck-Institute of Molecular Plant Physiology)

  • Heather E. McFarlane

    (University of Melbourne)

  • Anne Diehl

    (Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), NMR-supported Structural Biology)

  • Ghazanfar Abbas Khan

    (University of Melbourne)

  • Barth-Jan Rossum

    (Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), NMR-supported Structural Biology)

  • Edwin R. Lampugnani

    (University of Melbourne)

  • Witold G. Szymanski

    (Max-Planck-Institute of Molecular Plant Physiology)

  • Nils Cremer

    (Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), NMR-supported Structural Biology)

  • Peter Schmieder

    (Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), NMR-supported Structural Biology)

  • Kristina L. Ford

    (University of Melbourne)

  • Florian Seiter

    (Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), NMR-supported Structural Biology)

  • Joshua L. Heazlewood

    (University of Melbourne)

  • Clara Sanchez-Rodriguez

    (ETH Zurich)

  • Hartmut Oschkinat

    (Leibniz-Forschungsinstitut für Molekulare Pharmakologie (FMP), NMR-supported Structural Biology)

  • Staffan Persson

    (University of Melbourne
    Max-Planck-Institute of Molecular Plant Physiology)

Abstract

Microtubules are filamentous structures necessary for cell division, motility and morphology, with dynamics critically regulated by microtubule-associated proteins (MAPs). Here we outline the molecular mechanism by which the MAP, COMPANION OF CELLULOSE SYNTHASE1 (CC1), controls microtubule bundling and dynamics to sustain plant growth under salt stress. CC1 contains an intrinsically disordered N-terminus that links microtubules at evenly distributed points through four conserved hydrophobic regions. By NMR and live cell analyses we reveal that two neighboring residues in the first hydrophobic binding motif are crucial for the microtubule interaction. The microtubule-binding mechanism of CC1 is reminiscent to that of the prominent neuropathology-related protein Tau, indicating evolutionary convergence of MAP functions across animal and plant cells.

Suggested Citation

  • Christopher Kesten & Arndt Wallmann & René Schneider & Heather E. McFarlane & Anne Diehl & Ghazanfar Abbas Khan & Barth-Jan Rossum & Edwin R. Lampugnani & Witold G. Szymanski & Nils Cremer & Peter Sch, 2019. "The companion of cellulose synthase 1 confers salt tolerance through a Tau-like mechanism in plants," Nature Communications, Nature, vol. 10(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-08780-3
    DOI: 10.1038/s41467-019-08780-3
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    Cited by:

    1. Agnes Adler & Mamata Bangera & J. Wouter Beugelink & Salima Bahri & Hugo Ingen & Carolyn A. Moores & Marc Baldus, 2024. "A structural and dynamic visualization of the interaction between MAP7 and microtubules," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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