期刊
NATURE CELL BIOLOGY
卷 18, 期 10, 页码 1102-1108出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb3412
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- French National Agency for Research [ANR PCV06_142769, PCV07_190830]
- University of Rennes 1 (Emerging Scientific Challenges)
- Federative Research Institute Biosit (Innovative Scientific Project)
- Association for Cancer Research (Blank Program)
- Netherlands Organization for Scientific Research Aard-en-Levenswetenschapen VICI
- Swiss National Science Foundation [310030B_138659, 31003A_166608]
- German Research Foundation [SFB807, SPP1623]
- French Ministry of Education and Research
- French Association for Cancer Research (ARC)
- 'Ramon y Cajal' programme of the Spanish Ministry of Economy and Competitivity
- Marie Curie Career Integration Grant (EB-SxIP) [FP7-PEOPLE-2011-CIG-293831]
- European Molecular Biology Organization Long-Term Fellowship
- Marie Curie International Incoming Fellowship
EB1 is a microtubule plus-end tracking protein that recognizes GTP-tubulin dimers in microtubules(1-4) and thus represents a unique probe to investigate the architecture of the GTP cap of growing microtubule ends(5,6). 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.
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