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-Structure paper
タイトル | Structural insight into the intraflagellar transport complex IFT-A and its assembly in the anterograde IFT train. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 1506, Year 2023 |
掲載日 | 2023年3月17日 |
著者 | Yuanyuan Ma / Jun He / Shaobai Li / Deqiang Yao / Chenhui Huang / Jian Wu / Ming Lei / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:36932088 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.6 - 8.8 Å |
構造データ | EMDB-34893: elongated state of Tetrahymena IFT-A EMDB-34894: folded state of Tetrahymena IFT-A EMDB-34895, PDB-8hmc: EMDB-34896, PDB-8hmd: EMDB-34897, PDB-8hme: EMDB-34898, PDB-8hmf: EMDB-34899: head module state 3 of Tetrahymena IFT-A |
化合物 | ChemComp-ZN: |
由来 |
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キーワード | PROTEIN TRANSPORT / intraflagellar transport complex |