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Publication Abstract from PubMed

Intraflagellar transport (IFT) trains, the polymers composed of two multi-subunit complexes, IFT-A and IFT-B, carry out bidirectional intracellular transport in cilia, vital for cilia biogenesis and signaling. IFT-A plays crucial roles in the ciliary import of membrane proteins and the retrograde cargo trafficking. However, the molecular architecture of IFT-A and the assembly mechanism of the IFT-A into the IFT trains in vivo remains elusive. Here, we report the cryo-electron microscopic structures of the IFT-A complex from protozoa Tetrahymena thermophila. We find that IFT-A complexes present two distinct, elongated and folded states. Remarkably, comparison with the in situ cryo-electron tomography structure of the anterograde IFT train unveils a series of adjustments of the flexible arms in apo IFT-A when incorporated into the anterograde train. Our results provide an atomic-resolution model for the IFT-A complex and valuable insights into the assembly mechanism of anterograde IFT trains.

Structural insight into the intraflagellar transport complex IFT-A and its assembly in the anterograde IFT train.,Ma Y, He J, Li S, Yao D, Huang C, Wu J, Lei M Nat Commun. 2023 Mar 17;14(1):1506. doi: 10.1038/s41467-023-37208-2. PMID:36932088^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.