Figure 1.
Figure 1. CCEP-290 belongs to a third transition zone module required for assembly of the central cylinder. (A) Transition zone modules in C. elegans, based on genetic interactions and localization interdependencies (Huang et al., 2011; Williams et al., 2011; this study). (B) Modules in vertebrates, based on proteomic studies (green, red, blue: Sang et al., 2011; dark green: Chih et al., 2012; light green: Garcia-Gonzalo et al., 2011). *, C. elegans names used for ease of comparison. HGNC names: B9D1/MKSR1, B9D2/MKSR2, TMEM216/MKS2, TMEM67/MKS3, RPGRIP1L/MKS5, CC2D2A/MKS6. (C) Immunofluorescence micrographs of phasmid (tail) cilia of worms expressing GFP:CCEP-290 and stained for HYLS-1 and glutamylated tubulin. (D and E) Localization interdependencies between CCEP-290 and MKS/NPHP module components MKS-5, NPHP-4, and MKSR-2. Panels show phasmid cilia in worms coexpressing mCherry:HYLS1 and GFP:CCEP-290/MKSR-2/NPHP-4 in wild-type and transition zone mutants, as indicated. (F) MKSR-2 at transition zones is reduced due to dispersal along the ciliary axoneme. A still image and kymograph from a time-lapse sequence of GFP:MKSR-2 in ccep-290Δ mutant phasmids is shown (see also Video 1). The line indicates the kymograph axis. (G) Transmission electron micrographs of amphid transition zones in wild-type, ccep-290Δ, ccep-290Δ;nphp-4, and ccep-290;mksr-2;nphp-4 mutants. While a central cylinder is not apparent and transition zones are fragmented, Y-links (arrowheads) are still occasionally present in ccep-290Δ mutants. Inner singlet microtubule numbers are reduced (3.8 ± 1.5, n = 25 wild-type; 1.6 ± 1.4, n = 21 ccep-290Δ; t test; P < 0.0001), potentially due to loss of the central cylinder to which they normally attach. Transition zone structures are completely lost in ccep-290;mksr-2;nphp-4 triple mutants. Bars: (C, D, and E) 1 µm; (F) 5 µm; (G) 200 nm.

CCEP-290 belongs to a third transition zone module required for assembly of the central cylinder. (A) Transition zone modules in C. elegans, based on genetic interactions and localization interdependencies (Huang et al., 2011; Williams et al., 2011; this study). (B) Modules in vertebrates, based on proteomic studies (green, red, blue: Sang et al., 2011; dark green: Chih et al., 2012; light green: Garcia-Gonzalo et al., 2011). *, C. elegans names used for ease of comparison. HGNC names: B9D1/MKSR1, B9D2/MKSR2, TMEM216/MKS2, TMEM67/MKS3, RPGRIP1L/MKS5, CC2D2A/MKS6. (C) Immunofluorescence micrographs of phasmid (tail) cilia of worms expressing GFP:CCEP-290 and stained for HYLS-1 and glutamylated tubulin. (D and E) Localization interdependencies between CCEP-290 and MKS/NPHP module components MKS-5, NPHP-4, and MKSR-2. Panels show phasmid cilia in worms coexpressing mCherry:HYLS1 and GFP:CCEP-290/MKSR-2/NPHP-4 in wild-type and transition zone mutants, as indicated. (F) MKSR-2 at transition zones is reduced due to dispersal along the ciliary axoneme. A still image and kymograph from a time-lapse sequence of GFP:MKSR-2 in ccep-290Δ mutant phasmids is shown (see also Video 1). The line indicates the kymograph axis. (G) Transmission electron micrographs of amphid transition zones in wild-type, ccep-290Δ, ccep-290Δ;nphp-4, and ccep-290;mksr-2;nphp-4 mutants. While a central cylinder is not apparent and transition zones are fragmented, Y-links (arrowheads) are still occasionally present in ccep-290Δ mutants. Inner singlet microtubule numbers are reduced (3.8 ± 1.5, n = 25 wild-type; 1.6 ± 1.4, n = 21 ccep-290Δ; t test; P < 0.0001), potentially due to loss of the central cylinder to which they normally attach. Transition zone structures are completely lost in ccep-290;mksr-2;nphp-4 triple mutants. Bars: (C, D, and E) 1 µm; (F) 5 µm; (G) 200 nm.

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