Asymmetrically localized proteins stabilize basal bodies against ciliary beating forces
Author(s)
Bayless, Brian A.; Galati, Domenico F.; Junker, Anthony D.; Gaertig, Jacek; Pearson, Chad G.; Backer, Chelsea B.; ... Show more Show less
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Basal bodies are radially symmetric, microtubule-rich structures that nucleate and anchor motile cilia. Ciliary beating produces asymmetric mechanical forces that are resisted by basal bodies. To resist these forces, distinct regions within the basal body ultrastructure and the microtubules themselves must be stable. However, the molecular components that stabilize basal bodies remain poorly defined. Here, we determine that Fop1 functionally interacts with the established basal body stability components Bld10 and Poc1. We find that Fop1 and microtubule glutamylation incorporate into basal bodies at distinct stages of assembly, culminating in their asymmetric enrichment at specific triplet microtubule regions that are predicted to experience the greatest mechanical force from ciliary beating. Both Fop1 and microtubule glutamylation are required to stabilize basal bodies against ciliary beating forces. Our studies reveal that microtubule glutamylation and Bld10, Poc1, and Fop1 stabilize basal bodies against the forces produced by ciliary beating via distinct yet interdependent mechanisms.
Date issued
2016-11Department
Massachusetts Institute of Technology. Department of BiologyJournal
Journal of Cell Biology
Publisher
Rockefeller University Press, The
Citation
Bayless, Brian A.; Galati, Domenico F.; Junker, Anthony D.; Backer, Chelsea B.; Gaertig, Jacek and Pearson, Chad G. “Asymmetrically Localized Proteins Stabilize Basal Bodies Against Ciliary Beating Forces.” The Journal of Cell Biology 215, no. 4 (November 2016): 457–466. © 2016 Bayless et al
Version: Final published version
ISSN
0021-9525
1540-8140