AI Article Synopsis
- Intraflagellar transport (IFT) trains are complex molecular structures that transport proteins between cilia and the cell body, comprising IFT-A, IFT-B complexes, and motor proteins.
- Researchers reconstituted and analyzed the human IFT-A complex using cryo-electron microscopy, revealing how it polymerizes and interacts with IFT-B and TULP adaptor proteins to form "carriages."
- The study demonstrates that IFT-A·TULP carriages are critical for delivering various membrane proteins to cilia and regulating the IFT train's functions, linking IFT-A's roles to its evolutionary origins.
Article Abstract
Intraflagellar transport (IFT) trains are massive molecular machines that traffic proteins between cilia and the cell body. Each IFT train is a dynamic polymer of two large complexes (IFT-A and -B) and motor proteins, posing a formidable challenge to mechanistic understanding. Here, we reconstituted the complete human IFT-A complex and obtained its structure using cryo-EM. Combined with AlphaFold prediction and genome-editing studies, our results illuminate how IFT-A polymerizes, interacts with IFT-B, and uses an array of β-propeller and TPR domains to create "carriages" of the IFT train that engage TULP adaptor proteins. We show that IFT-A⋅TULP carriages are essential for cilia localization of diverse membrane proteins, as well as ICK-the key kinase regulating IFT train turnaround. These data establish a structural link between IFT-A's distinct functions, provide a blueprint for IFT-A in the train, and shed light on how IFT evolved from a proto-coatomer ancestor.
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| http://dx.doi.org/10.1016/j.cell.2022.11.010 | DOI Listing |
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