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-Structure paper
タイトル | Ciliary central apparatus structure reveals mechanisms of microtubule patterning. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 29, Issue 5, Page 483-492, Year 2022 |
掲載日 | 2022年5月16日 |
著者 | Miao Gui / Xiangli Wang / Susan K Dutcher / Alan Brown / Rui Zhang / |
PubMed 要旨 | A pair of extensively modified microtubules form the central apparatus (CA) of the axoneme of most motile cilia, where they regulate ciliary motility. The external surfaces of both CA microtubules ...A pair of extensively modified microtubules form the central apparatus (CA) of the axoneme of most motile cilia, where they regulate ciliary motility. The external surfaces of both CA microtubules are patterned asymmetrically with large protein complexes that repeat every 16 or 32 nm. The composition of these projections and the mechanisms that establish asymmetry and longitudinal periodicity are unknown. Here, by determining cryo-EM structures of the CA microtubules, we identify 48 different CA-associated proteins, which in turn reveal mechanisms for asymmetric and periodic protein binding to microtubules. We identify arc-MIPs, a novel class of microtubule inner protein, that bind laterally across protofilaments and remodel tubulin structure and lattice contacts. The binding mechanisms utilized by CA proteins may be generalizable to other microtubule-associated proteins. These structures establish a foundation to elucidate the contributions of individual CA proteins to ciliary motility and ciliopathies. |
リンク | Nat Struct Mol Biol / PubMed:35578023 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.7 - 3.8 Å |
構造データ | EMDB-25361: Composite map of ciliary C2 central pair apparatus isolated from Chlamydomonas reinhardtii EMDB-25381: Composite map of ciliary C1 central pair apparatus isolated from Chlamydomonas reinhardtii |
化合物 | ChemComp-GDP: ChemComp-GTP: ChemComp-MG: ChemComp-ADP: ChemComp-ANP: |
由来 |
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キーワード | STRUCTURAL PROTEIN / cilia / microtubule |