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Structural determinants of microtubule minus end preference in CAMSAP CKK domains

Author

Listed:
  • Joseph Atherton

    (University of London)

  • Yanzhang Luo

    (Utrecht University)

  • Shengqi Xiang

    (Utrecht University
    MOE Key Lab for biomolecular Condensates & Cellular Dynamics, School of Life Sciences, University of Science and Technology of China)

  • Chao Yang

    (Utrecht University)

  • Ankit Rai

    (Utrecht University)

  • Kai Jiang

    (Wuhan University)

  • Marcel Stangier

    (Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut)

  • Annapurna Vemu

    (Cell Biology and Biophysics Unit, National Institute of Neurological Disorders and Stroke)

  • Alexander D. Cook

    (University of London)

  • Su Wang

    (University of London)

  • Antonina Roll-Mecak

    (Cell Biology and Biophysics Unit, National Institute of Neurological Disorders and Stroke
    Biophysics Center, National Heart, Lung and Blood Institute)

  • Michel O. Steinmetz

    (Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut
    University of Basel, Biozentrum)

  • Anna Akhmanova

    (Utrecht University)

  • Marc Baldus

    (Utrecht University)

  • Carolyn A. Moores

    (University of London)

Abstract

CAMSAP/Patronins regulate microtubule minus-end dynamics. Their end specificity is mediated by their CKK domains, which we proposed recognise specific tubulin conformations found at minus ends. To critically test this idea, we compared the human CAMSAP1 CKK domain (HsCKK) with a CKK domain from Naegleria gruberi (NgCKK), which lacks minus-end specificity. Here we report near-atomic cryo-electron microscopy structures of HsCKK- and NgCKK-microtubule complexes, which show that these CKK domains share the same protein fold, bind at the intradimer interprotofilament tubulin junction, but exhibit different footprints on microtubules. NMR experiments show that both HsCKK and NgCKK are remarkably rigid. However, whereas NgCKK binding does not alter the microtubule architecture, HsCKK remodels its microtubule interaction site and changes the underlying polymer structure because the tubulin lattice conformation is not optimal for its binding. Thus, in contrast to many MAPs, the HsCKK domain can differentiate subtly specific tubulin conformations to enable microtubule minus-end recognition.

Suggested Citation

  • Joseph Atherton & Yanzhang Luo & Shengqi Xiang & Chao Yang & Ankit Rai & Kai Jiang & Marcel Stangier & Annapurna Vemu & Alexander D. Cook & Su Wang & Antonina Roll-Mecak & Michel O. Steinmetz & Anna A, 2019. "Structural determinants of microtubule minus end preference in CAMSAP CKK domains," Nature Communications, Nature, vol. 10(1), pages 1-16, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-13247-6
    DOI: 10.1038/s41467-019-13247-6
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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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