Structural determinants of microtubule minus end preference in CAMSAP CKK domains

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 Akhmanova, Marc Baldus () and Carolyn A. Moores ()
Additional contact information
Joseph Atherton: University of London
Yanzhang Luo: Utrecht University
Shengqi Xiang: Utrecht University
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
Michel O. Steinmetz: Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut
Anna Akhmanova: Utrecht University
Marc Baldus: Utrecht University
Carolyn A. Moores: University of London

Nature Communications, 2019, vol. 10, issue 1, 1-16

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-13247-6

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