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. 2017 Mar 1;28(5):624–633. doi: 10.1091/mbc.E16-09-0648

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© 2017 Funabashi, Katoh, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0).

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FIGURE 2: — Interaction of KIF17 with the IFT46–IFT56 dimer through its conserved C-terminal sequence. (A) Schematic representation of the overall structure and domain organization of KIF17 and alignment of the C-terminal sequences of human, mouse, and zebrafish KIF17 and C. elegans OSM-3. Coil1 and Coil2 are coiled-coil regions. Residues conserved in all and three members are shown in black and gray boxes, respectively. (B, C) Involvement of the conserved C-terminal sequence of KIF17 in its interaction with the IFT46–IFT56 dimer. Lysates prepared from HEK293T cells coexpressing mChe-IFT46 and mChe-IFT56 and EGFP-KIF17(WT), EGFP-KIF17(1-1018), EGFP-KIF17(1-1014), EGFP-KIF17(1-999), EGFP-KIF17(AAAA), or EGFP-KIF17(R1000/1003A) were subjected to the VIP assay (B) or immunoblotting analysis (C).