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The molecular structure of IFT-A and IFT-B in anterograde intraflagellar transport trains
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The molecular structure of IFT-A and IFT-B in anterograde intraflagellar transport trains
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Journal Article
The molecular structure of IFT-A and IFT-B in anterograde intraflagellar transport trains
2023
Overview
Anterograde intraflagellar transport (IFT) trains are essential for cilia assembly and maintenance. These trains are formed of 22 IFT-A and IFT-B proteins that link structural and signaling cargos to microtubule motors for import into cilia. It remains unknown how the IFT-A/-B proteins are arranged into complexes and how these complexes polymerize into functional trains. Here we use in situ cryo-electron tomography of
Chlamydomonas reinhardtii
cilia and AlphaFold2 protein structure predictions to generate a molecular model of the entire anterograde train. We show how the conformations of both IFT-A and IFT-B are dependent on lateral interactions with neighboring repeats, suggesting that polymerization is required to cooperatively stabilize the complexes. Following three-dimensional classification, we reveal how IFT-B extends two flexible tethers to maintain a connection with IFT-A that can withstand the mechanical stresses present in actively beating cilia. Overall, our findings provide a framework for understanding the fundamental processes that govern cilia assembly.
In situ cryo-electron tomography reveals the molecular structure of intraflagellar transport (IFT) protein complexes and their assembly into the anterograde IFT trains that build cilia.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
