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  • Structure Watch
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Structure watch

Nature Reviews Molecular Cell Biology volume 11, page 820 (2010)Cite this article

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The dynamic turnover of microtubule filaments, which consist of protofilaments of α-tubulin–β-tubulin heterodimers that are bound head-to-tail, is controlled by microtubule-associated proteins (MAPs). MAPs can either stabilize or destabilize microtubules, but our understanding of the mechanistic basis of this is limited by a lack of structural insights into how MAPs associate with microtubules. Fourniol et al. have now used cryo-electron microscopy and single particle algorithms to visualize how the MAP doublecortin (DCX) binds microtubules.

DCX can both nucleate and stabilize microtubules, which allowed Fourniol et al. to visualize microtubules assembled into the same architecture that they would form in vivo. They confirmed that these microtubules are made of a standard 13-protofilament cylinder and that DCX binds at the region where four tubulin dimers meet; this allows it to stabilize interactions along both the longitudinal and lateral lattices. DCX does not bind along the 'seam' — an area of discontinuity in the lattice that is proposed to affect microtubule dynamics — and this suggests that the way in which DCX stabilizes microtubules is not through this region.

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ORIGINAL RESEARCH PAPERS

  1. Fourniol, F. J. et al. Template-free 13-protofilament microtubule-MAP assembly visualized at 8 Å resolution. J. Cell Biol. 191, 463–470 (2010) Article

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  2. Güttler, T. et al. NES consensus redefined by structures of PKI-type and Rev-type nuclear export signals bound to CRM1. Nature Struct. Mol. Biol. 17, 1367–1376 (2010)

    Article  Google Scholar 

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Structure watch. Nat Rev Mol Cell Biol 11, 820 (2010). https://doi.org/10.1038/nrm3021

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