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-Structure paper
タイトル | EB1 interacts with outwardly curved and straight regions of the microtubule lattice. |
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ジャーナル・号・ページ | Nat Cell Biol, Vol. 18, Issue 10, Page 1102-1108, Year 2016 |
掲載日 | 2016年9月12日 |
著者 | Audrey Guesdon / Franck Bazile / Rubén M Buey / Renu Mohan / Solange Monier / Ruddi Rodríguez García / Morgane Angevin / Claire Heichette / Ralph Wieneke / Robert Tampé / Laurence Duchesne / Anna Akhmanova / Michel O Steinmetz / Denis Chrétien / |
PubMed 要旨 | EB1 is a microtubule plus-end tracking protein that recognizes GTP-tubulin dimers in microtubules and thus represents a unique probe to investigate the architecture of the GTP cap of growing ...EB1 is a microtubule plus-end tracking protein that recognizes GTP-tubulin dimers in microtubules and thus represents a unique probe to investigate the architecture of the GTP cap of growing microtubule ends. Here, we conjugated EB1 to gold nanoparticles (EB1-gold) and imaged by cryo-electron tomography its interaction with dynamic microtubules assembled in vitro from purified tubulin. EB1-gold forms comets at the ends of microtubules assembled in the presence of GTP, and interacts with the outer surface of curved and straight tubulin sheets as well as closed regions of the microtubule lattice. Microtubules assembled in the presence of GTP, different GTP analogues or cell extracts display similarly curved sheets at their growing ends, which gradually straighten as their protofilament number increases until they close into a tube. Together, our data provide unique structural information on the interaction of EB1 with growing microtubule ends. They further offer insights into the conformational changes that tubulin dimers undergo during microtubule assembly and the architecture of the GTP-cap region. |
リンク | Nat Cell Biol / PubMed:27617931 |
手法 | EM (トモグラフィー) |
構造データ | EMDB-2912: EMDB-2915: EMDB-2916: EMDB-2918: EMDB-2919: EMDB-2920: EMDB-2921: |
由来 |
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