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

Atherton, J; Jiang, K; Stangier, MM; Luo, Y; Hua, S; Houben, K; van Hooff, JJE; ... Akhmanova, A; + view all (2017) A structural model for microtubule minus-end recognition and protection by CAMSAP proteins. Nature Structural & Molecular Biology , 24 (11) pp. 931-943. 10.1038/nsmb.3483. Green open access

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Abstract

CAMSAP and Patronin family members regulate microtubule minus-end stability and localization and thus organize noncentrosomal microtubule networks, which are essential for cell division, polarization and differentiation. Here, we found that the CAMSAP C-terminal CKK domain is widely present among eukaryotes and autonomously recognizes microtubule minus ends. Through a combination of structural approaches, we uncovered how mammalian CKK binds between two tubulin dimers at the interprotofilament interface on the outer microtubule surface. In vitro reconstitution assays combined with high-resolution fluorescence microscopy and cryo-electron tomography suggested 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 interprotofilament interface at this site serve as 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.

Type: Article
Title: A structural model for microtubule minus-end recognition and protection by CAMSAP proteins
Open access status: An open access version is available from UCL Discovery
DOI: 10.1038/nsmb.3483
Publisher version: https://doi.org/10.1038/nsmb.3483
Language: English
Additional information: This version is the author accepted manuscript. For information on re-use, please refer to the publisher’s terms and conditions.
Keywords: Science & Technology, Life Sciences & Biomedicine, Biochemistry & Molecular Biology, Biophysics, Cell Biology, CRYOELECTRON MICROSCOPY, BINDING-PROTEIN, BETA-TUBULIN, DYNAMICS, RESOLUTION, PATRONIN, SPECTROSCOPY, ORGANIZATION, TRANSITIONS, KINESINS
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences > Structural and Molecular Biology
URI: http://discovery.ucl.ac.uk/id/eprint/10073509
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