Chlamydomonas IFT172 Is Encoded by FLA11, Interacts with CrEB1, and Regulates IFT at the Flagellar Tip
نویسندگان
چکیده
The transport of flagellar precursors and removal of turnover products from the flagellar tip is mediated by intraflagellar transport (IFT) , which is essential for both flagellar assembly and maintenance . Large groups of IFT particles are moved from the flagellar base to the tip by kinesin-2, and smaller groups are returned to the base by cytoplasmic dynein 1b. The IFT particles are composed of two protein complexes, A and B, comprising approximately 16-18 polypeptides. How cargo is unloaded from IFT particles, turnover products loaded, and active IFT motors exchanged at the tip is unknown. We previously showed that the Chlamydomonas microtubule end binding protein 1 (CrEB1) localizes to the flagellar tip and is depleted from the tips of the temperature-sensitive (ts) mutant fla11ts . We demonstrate here that FLA11 encodes IFT protein 172, a component of IFT complex B, and show that IFT172 interacts with CrEB1. Because fla11ts cells are defective in IFT particle turnaround at the tip, our results indicate that IFT172 is involved in regulating the transition between anterograde and retrograde IFT at the tip, perhaps by a mechanism involving CrEB1. Therefore, IFT172 is involved in the control of flagellar assembly/disassembly at the tip.
منابع مشابه
The Microtubule Plus End-Tracking Protein EB1 Is Localized to the Flagellar Tip and Basal Bodies in Chlamydomonas reinhardtii
Flagellar axonemes assemble and continuously turn over at the flagellar tip. The supply and removal of axonemal subunits at the tip are mediated by intraflagellar transport (IFT), a motility process essential for the assembly and maintenance of all eukaryotic flagella and cilia. IFT is characterized by the movement of large protein complexes (IFT particles) from the basal bodies to the flagella...
متن کاملCells in D.C.: The American Society for Cell Biology
IFT172 turns traffic around lagella and cilia are constantly turning over proteins at their tips. Assembly at the tip and removal of turnover products require the intraflagellar transport (IFT) system, which uses axonemal microtubules as tracks to drop off flagellar tip proteins and return turnover products to the cell body. The change in IFT direction at the tip was discussed by Lotte Pedersen...
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The microtubule (MT) +-end tracking protein EB1 is present at the tip of cilia and flagella; EB1 remains at the tip during flagellar shortening and in the absence of intraflagellar transport (IFT), the predominant protein transport system in flagella. To investigate how EB1 accumulates at the http://www.molbiolcell.org/content/suppl/2015/11/30/mbc.E15-08-0608v1.DC1 Supplemental Material can be ...
متن کاملSingle-particle imaging reveals intraflagellar transport-independent transport and accumulation of EB1 in Chlamydomonas flagella.
The microtubule (MT) plus-end tracking protein EB1 is present at the tips of cilia and flagella; end-binding protein 1 (EB1) remains at the tip during flagellar shortening and in the absence of intraflagellar transport (IFT), the predominant protein transport system in flagella. To investigate how EB1 accumulates at the flagellar tip, we used in vivo imaging of fluorescent protein-tagged EB1 (E...
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Assembly of cilia and flagella requires intraflagellar transport (IFT), a highly regulated kinesin-based transport system that moves cargo from the basal body to the tip of flagella [1]. The recruitment of IFT components to basal bodies is a function of flagellar length, with increased recruitment in rapidly growing short flagella [2]. The molecular pathways regulating IFT are largely a mystery...
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ورودعنوان ژورنال:
- Current Biology
دوره 15 شماره
صفحات -
تاریخ انتشار 2005