Figure 4. C. elegans DYF-11::GFP may be functionally associated with IFT particle subcomplex B. (A, B) DYF-11::GFP localizes along the entire length of amphid/phasmid cilia in wild-type (N2) and klp-11
(a motor component of heterotrimeric Kinesin-2) animals, both of which have full-length cilia. Note the schematics at the bottom of the figure. (C) DYF-11::GFP is observed along the length of the middle segments of osm-3
(homodimeric Kinesin-2) mutants, which lack the distal segments (see schematic). (D-F) DYF-11::GFP localizes along the entire middle segments and truncated distal segments of bbs mutant worms, consistent with the hypothesis that DYF-11 is associated with OSM-3-kinesin/IFT subcomplex B (Kinesin-II/subcomplex A does not enter the distal segment; see schematic). Middle segments (MS) and distal segments (DS) are specifically highlighted. (G, H) DYF-11::GFP ciliary localization is not perturbed in the truncated cilia of two subcomplex B mutants (che-13
, respectively; see schematic). Transition zones (TZ) are shown by white arrowheads, unusual dendritic termini are denoted by hollow arrowheads, and brackets designate the observed ciliary axonemes. Note that DYF-11 behaves like an IFT subcomplex B component (i.e., moves into the cilia of osm-3
as well as distal segment of bbs mutants). Scale bar, 5 um. (I) Kymograph analyses show the movement of DYF-11::GFP in a bbs-7
mutant animal at a velocity of 1.21±0.19 μm/sec along the middle and distal segments of phasmid cilia, consistent with an association with OSM-3-kinesin.