Molecular Basis of Tubulin Transport Within the Cilium by IFT74 and IFT81
Sagar Bhogaraju(Max Planck Institute of Biochemistry), Lukáš Čajánek(University of Basel), Cécile Fort(Centre National de la Recherche Scientifique), Thierry Blisnick(Centre National de la Recherche Scientifique), Kristina Weber(Max Planck Institute of Biochemistry), Michael Täschner(Max Planck Institute of Biochemistry), Naoko Mizuno(Max Planck Institute of Biochemistry), Stefan Lamla(Max Planck Institute of Biochemistry), Philippe Bastin(Centre National de la Recherche Scientifique), Erich A. Nigg(University of Basel), Esben Lorentzen(Max Planck Institute of Biochemistry)
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Abstract
Intraflagellar transport (IFT) of ciliary precursors such as tubulin from the cytoplasm to the ciliary tip is involved in the construction of the cilium, a hairlike organelle found on most eukaryotic cells. However, the molecular mechanisms of IFT are poorly understood. Here, we found that the two core IFT proteins IFT74 and IFT81 form a tubulin-binding module and mapped the interaction to a calponin homology domain of IFT81 and a highly basic domain in IFT74. Knockdown of IFT81 and rescue experiments with point mutants showed that tubulin binding by IFT81 was required for ciliogenesis in human cells.
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