Publication Date
2019
Journal or Book Title
Cytoskeleton
Abstract
Microtubule network remodeling is an essential process for cell development, maintenance, cell division, and motility. Microtubule‐severing enzymes are key players in the remodeling of the microtubule network; however, there are still open questions about their fundamental biochemical and biophysical mechanisms. Here, we explored the ability of the microtubule‐severing enzyme katanin to depolymerize stabilized microtubules. Interestingly, we found that the tubulin C‐terminal tail (CTT), which is required for severing, is not required for katanin‐catalyzed depolymerization. We also found that the depolymerization of microtubules lacking the CTT does not require ATP or katanin's ATPase activity, although the ATP turnover enhanced depolymerization. We also observed that the depolymerization rate depended on the katanin concentration and was best described by a hyperbolic function. Finally, we demonstrate that katanin can bind to filaments that lack the CTT, contrary to previous reports. The results of our work indicate that microtubule depolymerization likely involves a mechanism in which binding, but not enzymatic activity, is required for tubulin dimer removal from the filament ends.
ORCID
https://orcid.org/0000-0002-4838-3798
DOI
https://doi.org/10.1002/cm.21522
Pages
254-268
Volume
76
Issue
3
License
UMass Amherst Open Access Policy
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.
Funder
Division of Materials Research, Grant/Award Numbers: 1207783, 1359191; Division of Molecular and Cellular Biosciences, Grant/Award Number: 1817926; National Institute of General Medical Sciences, Grant/Award Number: R01 GM109909
Recommended Citation
Belonogov, Liudmila; Bailey, Megan E.; Tyler, Madison A.; Kazemi, Arianna; and Ross, Jennifer L., "Katanin catalyzes microtubule depolymerization independently of tubulin C-terminal tails" (2019). Cytoskeleton. 1254.
https://doi.org/10.1002/cm.21522