IFT54 directly interacts with kinesin‐II and IFT dynein to regulate anterograde intraflagellar transport |
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| Authors: | Xin Zhu Jieling Wang Shufen Li Karl Lechtreck Junmin Pan |
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| Affiliation: | 1. MOE Key Laboratory of Protein Sciences, Tsinghua‐Peking Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing China ; 2. Laboratory for Marine Biology and Biotechnology, Qingdao National Laboratory for Marine Science and Technology, Qingdao Shandong Province, China ; 3. Department of Cellular Biology, University of Georgia, Athens GA, USA |
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| Abstract: | The intraflagellar transport (IFT) machinery consists of the anterograde motor kinesin‐II, the retrograde motor IFT dynein, and the IFT‐A and ‐B complexes. However, the interaction among IFT motors and IFT complexes during IFT remains elusive. Here, we show that the IFT‐B protein IFT54 interacts with both kinesin‐II and IFT dynein and regulates anterograde IFT. Deletion of residues 342–356 of Chlamydomonas IFT54 resulted in diminished anterograde traffic of IFT and accumulation of IFT motors and complexes in the proximal region of cilia. IFT54 directly interacted with kinesin‐II and this interaction was strengthened for the IFT54Δ342–356 mutant in vitro and in vivo. The deletion of residues 261–275 of IFT54 reduced ciliary entry and anterograde traffic of IFT dynein with accumulation of IFT complexes near the ciliary tip. IFT54 directly interacted with IFT dynein subunit D1bLIC, and deletion of residues 261–275 reduced this interaction. The interactions between IFT54 and the IFT motors were also observed in mammalian cells. Our data indicate a central role for IFT54 in binding the IFT motors during anterograde IFT. |
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| Keywords: | cilia, flagella, IFT dynein, IFT54, intraflagellar transport, kinesin‐ II |
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