Rxivist logo

Structural determinants of microtubule minus end preference in CAMSAP CKK domains

By Joseph Atherton, Yanzhang Luo, Shengqi Xiang, Chao Yang, Kai Jiang, Marcel Stangier, Annapurna Vemu, Alexander D Cook, Su Wang, Antonina Roll-Mecak, Michel O. Steinmetz, Anna Akhmanova, Marc Baldus, Carolyn A Moores

Posted 27 Mar 2019
bioRxiv DOI: 10.1101/586230 (published DOI: 10.1038/s41467-019-13247-6)

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 has lost minus-end specificity. Near-atomic cryo-electron microscopy structures of HsCKK- and NgCKK-microtubule complexes show that these CKK domains share the same protein fold, bind at the intradimer interprotofilament tubulin junction, but exhibit subtly different footprints on microtubules. 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. NMR experiments show that HsCKK is remarkably rigid, supporting this remodelling ability. Thus, in contrast to many MAPs, CKK domains can differentiate subtly specific tubulin conformations to enable microtubule minus-end recognition.

Download data

  • Downloaded 623 times
  • Download rankings, all-time:
    • Site-wide: 50,703
    • In biophysics: 1,650
  • Year to date:
    • Site-wide: 157,875
  • Since beginning of last month:
    • Site-wide: 146,761

Altmetric data

Downloads over time

Distribution of downloads per paper, site-wide