8bda: Difference between revisions
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==IFTA complex in anterograde | ==IFTA complex in anterograde intraflagellar transport trains (Chlamydomonas reinhardtii)== | ||
<StructureSection load='8bda' size='340' side='right'caption='[[8bda]], [[Resolution|resolution]] 20.70Å' scene=''> | <StructureSection load='8bda' size='340' side='right'caption='[[8bda]], [[Resolution|resolution]] 20.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
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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. | 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. | ||
The molecular structure of IFT-A and IFT-B in anterograde intraflagellar transport trains.,Lacey SE, Foster HE, Pigino G Nat Struct Mol Biol. 2023 | The molecular structure of IFT-A and IFT-B in anterograde intraflagellar transport trains.,Lacey SE, Foster HE, Pigino G Nat Struct Mol Biol. 2023 May;30(5):584-593. doi: 10.1038/s41594-022-00905-5. , Epub 2023 Jan 2. PMID:36593313<ref>PMID:36593313</ref> | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
