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.
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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 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: | https://discovery.ucl.ac.uk/id/eprint/10073509 |
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