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Drosophila Katanin-60 Depolymerizes and Severs at Microtubule Defects
Journal of Cell Biology (2011)
  • Jennifer Ross, University of Massachusetts - Amherst
  • David J Sharp
  • Dong Zhang
  • Megan Bailey
  • Margaret M. Morelli
  • Juan Daniel Díaz-Valencia
Microtubule (MT) length and location is tightly controlled in cells. One novel family of MT-associated proteins that regulates MT dynamics is the MT-severing enzymes. In this work, we investigate how katanin (p60), believed to be the first discovered severing enzyme, binds and severs MTs via single molecule total internal reflection fluorescence microscopy. We find that severing activity depends on katanin concentration. We also find that katanin can remove tubulin dimers from the ends of MTs, appearing to depolymerize MTs. Strikingly, katanin localizes and severs at the interface of GMPCPP-tubulin and GDP-tubulin suggesting that it targets to protofilament-shift defects. Finally, we observe that binding duration, mobility, and oligomerization are ATP dependent.
Publication Date
May, 2011
Publisher Statement
This work is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License.
Citation Information
Jennifer Ross, David J Sharp, Dong Zhang, Megan Bailey, et al.. "Drosophila Katanin-60 Depolymerizes and Severs at Microtubule Defects" Journal of Cell Biology Vol. 100 Iss. 10 (2011)
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