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In vivo imaging shows continued association of several IFT-A, IFT-B and dynein complexes while IFT trains U-turn at the tip.

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Jordan,  Mareike A
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Pigino,  Gaia
Max Planck Institute for Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Wingfield, J. L., Mekonnen, B., Mengoni, I., Liu, P., Jordan, M. A., Diener, D. R., et al. (2021). In vivo imaging shows continued association of several IFT-A, IFT-B and dynein complexes while IFT trains U-turn at the tip. Journal of cell science, 134(18): jcs.259010. doi:10.1242/jcs.259010.


Cite as: https://hdl.handle.net/21.11116/0000-000A-0B95-2
Abstract
Flagellar assembly depends on intraflagellar transport (IFT), a bidirectional motility of protein carriers, the IFT trains. The trains are periodic assemblies of IFT-A and IFT-B subcomplexes and the motors kinesin-2 and IFT dynein. At the tip, anterograde trains are remodeled for retrograde IFT, a process that in Chlamydomonas involves kinesin-2 release and train fragmentation. However, the degree of train disassembly at the tip remains unknown. Here, we performed two-color imaging of fluorescent protein-tagged IFT components, which indicates that IFT-A and IFT-B proteins from a given anterograde train usually return in the same set of retrograde trains. Similarly, concurrent turnaround was typical for IFT-B proteins and the IFT dynein subunit D1bLIC-GFP but severance was observed as well. Our data support a simple model of IFT turnaround, in which IFT-A, IFT-B and IFT dynein typically remain associated at the tip and segments of the anterograde trains convert directly into retrograde trains. Continuous association of IFT-A, IFT-B and IFT dynein during tip remodeling could balance protein entry and exit, preventing the build-up of IFT material in flagella.