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    Structural determinants of microtubule minus end preference in CAMSAP CKK domains

    Atherton, J. and Luo, Y. and Xiang, S. and Yang, C. and Rai, A. and Jiang, K. and Stangier, M. and Vemu, A. and Cook, A.D. and Wang, S. and Roll-Mecak, A. and Steinmetz, M.O. and Akhmanova, A. and Baldus, M. and Moores, Carolyn A. (2019) Structural determinants of microtubule minus end preference in CAMSAP CKK domains. Nature Communications 10 (1), ISSN 2041-1723.

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    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.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Administrator
    Date Deposited: 20 Nov 2019 14:12
    Last Modified: 21 Nov 2019 08:34
    URI: http://eprints.bbk.ac.uk/id/eprint/30016

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