Drosophila katanin-60 depolymerizes and severs at microtubule defects

Juan Daniel Díaz-Valencia, Margaret M. Morelli, Megan Bailey, Dong Zhang, David J. Sharp, Jennifer L. Ross

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Abstract

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.

Original languageEnglish (US)
Pages (from-to)2440-2449
Number of pages10
JournalBiophysical Journal
Volume100
Issue number10
DOIs
StatePublished - May 18 2011

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ASJC Scopus subject areas

  • Biophysics

Cite this

Díaz-Valencia, J. D., Morelli, M. M., Bailey, M., Zhang, D., Sharp, D. J., & Ross, J. L. (2011). Drosophila katanin-60 depolymerizes and severs at microtubule defects. Biophysical Journal, 100(10), 2440-2449. https://doi.org/10.1016/j.bpj.2011.03.062