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-Structure paper
タイトル | The inner junction complex of the cilia is an interaction hub that involves tubulin post-translational modifications. |
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ジャーナル・号・ページ | Elife, Vol. 9, Year 2020 |
掲載日 | 2020年1月17日 |
著者 | Ahmad Abdelzaher Zaki Khalifa / Muneyoshi Ichikawa / Daniel Dai / Shintaroh Kubo / Corbin Steven Black / Katya Peri / Thomas S McAlear / Simon Veyron / Shun Kai Yang / Javier Vargas / Susanne Bechstedt / Jean-François Trempe / Khanh Huy Bui / |
PubMed 要旨 | Microtubules are cytoskeletal structures involved in stability, transport and organization in the cell. The building blocks, the α- and β-tubulin heterodimers, form protofilaments that associate ...Microtubules are cytoskeletal structures involved in stability, transport and organization in the cell. The building blocks, the α- and β-tubulin heterodimers, form protofilaments that associate laterally into the hollow microtubule. Microtubule also exists as highly stable doublet microtubules in the cilia where stability is needed for ciliary beating and function. The doublet microtubule maintains its stability through interactions at its inner and outer junctions where its A- and B-tubules meet. Here, using cryo-electron microscopy, bioinformatics and mass spectrometry of the doublets of and , we identified two new inner junction proteins, FAP276 and FAP106, and an inner junction-associated protein, FAP126, thus presenting the complete answer to the inner junction identity and localization. Our structural study of the doublets shows that the inner junction serves as an interaction hub that involves tubulin post-translational modifications. These interactions contribute to the stability of the doublet and hence, normal ciliary motility. |
リンク | Elife / PubMed:31951202 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.6 - 4.57 Å |
構造データ | EMDB-20855: 48-nm repeat unit of the doublet microtubule from Chlamydomonas reinhardtii EMDB-20856: EMDB-20858, PDB-6ve7: |
化合物 | ChemComp-GTP: ChemComp-MG: ChemComp-GDP: ChemComp-TA1: |
由来 |
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キーワード | STRUCTURAL PROTEIN / cilia / doublet / axoneme / microtubule inner protein |