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    A structural model for microtubule minus-end recognition and protection by CAMSAP proteins

    Atherton, Joe and Jiang, K. and Stangier, M.M. and Luo, Y. and Hua, S. and Houben, K. and von Hooff, J.J.E. and Joseph, Agnel Praveen and Scarabelli, G. and Grant, B.J. and Roberts, Anthony and Topf, Maya and Steinmetz, M. and Baldus, M. and Moores, Carolyn A. and Akhmanova, A. (2017) A structural model for microtubule minus-end recognition and protection by CAMSAP proteins. Nature Structural and Molecular Biology 24 , pp. 931-943. ISSN 1545-9993.

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    Abstract

    CAMSAP and Patronin family members regulate microtubule minus-end stability and localization and thus organize non-centrosomal microtubule networks, which are essential for cell division, polarization and differentiation. Here, we show that the C-terminal CKK domain of CAMSAPs is widely present among eukaryotes and autonomously recognizes microtubule minus ends. Through a combination of structural approaches, we uncover how mammalian CKK binds between two tubulin dimers at the inter-protofilament interface on the outer microtubule surface. In vitro reconstitution assays combined with high resolution fluorescence microscopy and cryo-electron tomography suggest that CKK preferentially associates with the transition zone between curved protofilaments and the regular microtubule lattice. We propose that minus-end-specific features of the inter-protofilament interface at this site form the basis for CKK’s minus-end preference. The steric clash between microtubule-bound CKK and kinesin motors explains how CKK protects microtubule minus ends against kinesin-13-induced depolymerization and thus controls the stability of free microtubule minus ends.

    Metadata

    Item Type: Article
    Keyword(s) / Subject(s): microtubules, CAMSAP, patronin, cytoskeleton, cryo-EM
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Carolyn Moores
    Date Deposited: 09 Oct 2017 15:43
    Last Modified: 10 Apr 2018 00:10
    URI: http://eprints.bbk.ac.uk/id/eprint/19810

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