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Fort, C, Collingridge, P, Brownlee, C and Wheeler, G 2020 Ca2+ elevations disrupt interactions between intraflagellar transport and the flagella membrane in Chlamydomonas. Journal of Cell Science, 134 (3). https://doi.org/10.1242/jcs.253492
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47 Ca2+ elevations disrupt interactions between intraflagellar transport and the flagella membrane in Chlamydomonas.pdf - Published Version Available under License Creative Commons Attribution. Download (9MB) | Preview |
Abstract/Summary
The movement of ciliary membrane proteins is directed by transient interactions with intraflagellar transport (IFT) trains. The green alga Chlamydomonas has adapted this process for gliding motility, using retrograde IFT motors to move adhesive glycoproteins in the flagella membrane. Ca2+ signalling contributes directly to the gliding process, although uncertainty remains over the mechanism through which it acts. Here, we show that flagella Ca2+ elevations initiate the movement of paused retrograde IFT trains, which accumulate at the distal end of adherent flagella, but do not influence other IFT processes. On highly adherent surfaces, flagella exhibit high frequency Ca2+ elevations that prevent the accumulation of paused retrograde IFT trains. Flagella Ca2+ elevations disrupt the IFT dependent movement of microspheres along the flagella membrane, suggesting that Ca2+ acts by directly disrupting an interaction between retrograde IFT trains and flagella membrane glycoproteins. By regulating the extent to which glycoproteins on the flagella surface interact with IFT motor proteins on the axoneme, this signalling mechanism allows precise control of traction force and gliding motility in adherent flagella.
| Item Type: | Publication - Article |
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| Additional Keywords: | Chlamydomonas, Ca2+ signalling, Intraflagellar transport |
| Subjects: | Marine Sciences |
| Divisions: | Marine Biological Association of the UK > Marine Microbiome |
| Depositing User: | Emily Smart |
| Date made live: | 20 Aug 2021 11:09 |
| Last Modified: | 09 Feb 2024 17:08 |
| URI: | https://plymsea.ac.uk/id/eprint/9322 |
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