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. 2016 May 13;7:11491. doi: 10.1038/ncomms11491

Figure 3. Identification of IFT-B sub-complexes and edgetic variants.

Figure 3

(a) Socioaffinity-weighted, spring-embedded (cytoscape) layout of IFT-B proteins with two sub-complexes indicated. (b) Cumulative elution profiles for IFT-B1/B2 proteins FLAG-purified and analysed by EPASIS in HEK293 cells stably expressing IFT88 or IFT27. Green and blue lines show components of IFT-B1 and -B2 sub-complexes, respectively. (c) Networks showing protein depletions in IFT-B comparing mutant to wild type with TAP-MS. Red arrows denote proteins with variants, and protein size is proportional negative fold-change. Top left, IFT88 p.R607H, a heterozygous MKS patient variant leads to a loss of IFT-B1. Bottom left, HSPB11 p.T41I (heterozygous MKS) at the IFT27 interface, leads to the loss of IFT-B1. Top right, IFT-B2 subunit, IFT172 p.E1153G (heterozygous in MKS) leads to a loss of IFT-B2. Bottom right, HSPB11 p.R61S (heterozygous JATD), on the surface, potentially interacting with an unknown partner, though not at any known interface affects only HSPB11 itself. Green and blue nodes represent components of the IFT-B1 and -B2 sub-complexes, respectively.