ArticleCytoskeleton (Hoboken, N.J.)2019
Katanin catalyzes microtubule depolymerization independently of tubulin C-terminal tails.
Article in Cytoskeleton (Hoboken, N.J.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 15 citations in OpenAlex.
- Epsilon tubulin is an essential determinant of microtubule-based structures in male germ cells.EMBO reports · 2024Article
- Article
- A Tale of 12 Tails: Katanin Severing Activity Affected by Carboxy-Terminal Tail Sequences.Biomolecules · 2023Article
- CsKTN1 for a katanin p60 subunit is associated with the regulation of fruit elongation in cucumber (Cucumis sativus L.).TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2021Article
- The Mammalian Family of Katanin Microtubule-Severing Enzymes.Frontiers in cell and developmental biology · 2021Review
- The model of local axon homeostasis - explaining the role and regulation of microtubule bundles in axon maintenance and pathology.Neural development · 2019Review
- Katanin catalyzes microtubule depolymerization independently of tubulin C-terminal tails.Cytoskeleton (Hoboken, N.J.) · 2019Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.