期刊
JOURNAL OF CELL SCIENCE
卷 134, 期 18, 页码 -出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jcs.259010
关键词
Cilia; Dynein1b; Kinesin-2; BBSome; Flagella
类别
资金
- National Institutes of Health [R01GM110413]
- Max Planck Society
- Human Technopole
- European Research Council (ERC) under the European Union [819826]
- University of Georgia (UGA) CURO Research Assistantship for undergraduate researchers
- European Research Council (ERC) [819826] Funding Source: European Research Council (ERC)
The study utilized two-color imaging of fluorescent protein-tagged IFT components to show that IFT-A and IFT-B proteins from a given anterograde train usually return in the same set of retrograde trains. Additionally, concurrent turnaround was typical for IFT-B proteins and the IFT dynein subunit D1 bLIC-GFP, but severance was also observed.
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 D1 bLIC-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.
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