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Structural determinants of microtubule minus end preference in CAMSAP CKK domains.
- Source :
-
Nature communications [Nat Commun] 2019 Nov 20; Vol. 10 (1), pp. 5236. Date of Electronic Publication: 2019 Nov 20. - Publication Year :
- 2019
-
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.
- Subjects :
- Cryoelectron Microscopy
Humans
Magnetic Resonance Spectroscopy
Microtubule-Associated Proteins metabolism
Microtubules metabolism
Models, Molecular
Naegleria metabolism
Protein Binding
Protein Domains
Tubulin metabolism
Microtubule-Associated Proteins ultrastructure
Microtubules ultrastructure
Naegleria ultrastructure
Tubulin ultrastructure
Subjects
Details
- Language :
- English
- ISSN :
- 2041-1723
- Volume :
- 10
- Issue :
- 1
- Database :
- MEDLINE
- Journal :
- Nature communications
- Publication Type :
- Academic Journal
- Accession number :
- 31748546
- Full Text :
- https://doi.org/10.1038/s41467-019-13247-6