ArticleThe Journal of biological chemistry2015
Microtubule severing by katanin p60 AAA+ ATPase requires the C-terminal acidic tails of both α- and β-tubulins and basic amino acid residues in the AAA+ ring pore.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 41 citations in OpenAlex.
- Computational perspectives on tubulin E-hook structure and mechanisms.Biophysical reports · 2026Review
- Fertility is compromised after oocyte-specific deletion of microtubule severing protein Katanin A1.Molecular human reproduction · 2025Article
- Piezoelectric biosensors: shedding light on principles and applications.Mikrochimica acta · 2024Review
- AAA+ protease-adaptor structures reveal altered conformations and ring specialization.Nature structural & molecular biology · 2022Article
- Fidgetin knockdown and knockout influences female reproduction distinctly in mice.Journal of biomedical research · 2022Article
- 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
- Cutting, Amplifying, and Aligning Microtubules with Severing Enzymes.Trends in cell biology · 2021Review
- Katanin Grips the β-Tubulin Tail through an Electropositive Double Spiral to Sever Microtubules.Developmental cell · 2020Article
- The molecular principles governing the activity and functional diversity of AAA+ proteins.Nature reviews. Molecular cell biology · 2020Review
- A Mechanistic Perspective on PEX1 and PEX6, Two AAA+ Proteins of the Peroxisomal Protein Import Machinery.International journal of molecular sciences · 2019Review
- Katanin catalyzes microtubule depolymerization independently of tubulin C-terminal tails.Cytoskeleton (Hoboken, N.J.) · 2019Article
- Microtubule-severing enzymes: From cellular functions to molecular mechanism.The Journal of cell biology · 2018Review
- Peroxisomal monoubiquitinated PEX5 interacts with the AAA ATPases PEX1 and PEX6 and is unfolded during its dislocation into the cytosol.The Journal of biological chemistry · 2018Article
- Motor axon navigation relies on Fidgetin-like 1-driven microtubule plus end dynamics.The Journal of cell biology · 2018Article
- The role of katanin p60 in breast cancer bone metastasis.Oncology letters · 2018Article
- Katanin-like 2 (KATNAL2) functions in multiple aspects of haploid male germ cell development in the mouse.PLoS genetics · 2017Article
- Katanin spiral and ring structures shed light on power stroke for microtubule severing.Nature structural & molecular biology · 2017Article
- Deviation of the typical AAA substrate-threading pore prevents fatal protein degradation in yeast Cdc48.Scientific reports · 2017Article
- Engineered AAA+ proteases reveal principles of proteolysis at the mitochondrial inner membrane.Nature communications · 2016Article
- Meiotic Clade AAA ATPases: Protein Polymer Disassembly Machines.Journal of molecular biology · 2016Review
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The microtubule (MT) network is highly dynamic and undergoes dramatic reorganizations during the cell cycle. Dimers of α- and β-tubulins rapidly polymerize to and depolymerize from the end of MT fibrils in an intrinsic GTP-dependent manner. MT severing by ATP-driven enzymes such as katanin and spastin contributes significantly to microtubule dynamics, and it has been shown that katanin p60, a AAA+ family protein, has ATPase and MT-severing activities. The mechanism of MT severing by katanin p60 is poorly understood, and the residues in katanin p60 and tubulins important for severing activity were therefore explored in this study. MT-severing activity, but not ATPase activity, was inhibited by mutations of the conserved aromatic residue and the flanking basic residues in the pore region of the katanin p60 hexameric ring. When the acidic residue-rich C-terminal unstructured segment of either α- or β-tubulin was removed, polymerized MTs were resistant to katanin p60 treatment. Interactions between katanin p60 and the mutant MTs, on the other hand, were unaffected. Taken together, these findings led us to propose that the interactions between the positively charged residues of katanin p60 and the acidic tails of both tubulins are essential for efficient severing of MTs.
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