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Figure 9


Fig. 9. Model of the retrograde IFT dynein motor. This model for associations involving the IFT dynein is based on the gel filtration, immunoprecipitation and sucrose-gradient data presented here. D1bLIC and an IC-LC complex, consisting of a FAP133 and an LC8 dimer, are predicted to associate independently with the N-terminal region of the DHC1b homodimer. The FAP133-LC8 subunit may mediate loading of the dynein motor complex onto an IFT particle scaffold that includes the FLA10 kinesin-2 subunit, complex A protein IFT139 and possibly complex B. Upon gel filtration, this dynein–kinesin-2–IFT complex assembly has a mass greater than that of the ~2 MDa outer dynein arm. Such IFT assemblies can dissociate into smaller complexes including intact dynein motors, IFT complex A, IFT complex B and heterotrimeric kinesin-2. The FAP133/LC8 subunit can further detach from the dynein complex and subsequently the DHC1b dimer may also dissociate to yield single HCs. It is currently unknown whether one D1bLIC remains bound to each DHC1b monomer or whether some HCs have two D1bLICs associated and others none.





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