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. 2017 Feb 16;13(2):e1006627. doi: 10.1371/journal.pgen.1006627

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© 2017 Zhu et al

This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

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Fig 2 — (A) Loss of IFT43 decreases the cellular levels of IFT-A proteins. Whole cell lysates were probed by immunoblotting with the antibodies indicated. IC69 was used as a control. (B) Loss of IFT43 does not affect the cellular levels of IFT-B and IFT motors. Whole cell lysates from indicated cells were analyzed by immunoblotting. CDPK3, a calcium dependent kinase 3, was used as a loading control. (C) Loss of IFT43 apparently leads to formation of a smaller IFT-A complex containing IFT144, IFT140, IFT122, and IFT121. Whole cell lysates were subjected to sucrose gradient sedimentation analysis followed by immunoblot analysis. Arrows indicate the peak of the IFT-A complex in WT and ift43 cells. (D) IFT43 regulates the cellular levels of IFT-A proteins via protein degradation. WT and ift43 cells were treated with proteasome inhibitor MG-132 for different times followed by immunoblotting. (E) The integrity of IFT-A complex in IFT-A stability. Cell lysates from all IFT-A mutants were probed via immunoblots. Please note that the ift144 mutant is not a null mutant.