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, Carolyn A Moores

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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.
Original languageEnglish
Article number5236
Pages (from-to)1-16
JournalNature Communications
Early online date20 Nov 2019
Publication statusPublished - 20 Nov 2019


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