ArticleDevelopmental cell2020
Katanin Grips the β-Tubulin Tail through an Electropositive Double Spiral to Sever Microtubules.
Article in Developmental cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 80 citations in OpenAlex.
- Differential contributions of β-tubulin isotypes to acentrosomal oocyte meiosis in C. elegans.The Journal of cell biology · 2026Article
- Molecular Insights Into the Differential Binding Affinity of Human Katanin Hexamer for C-Terminal Tails of β-Tubulin Isotypes.Cytoskeleton (Hoboken, N.J.) · 2026Article
- Missense variants in KATNA1 alter microtubule dynamics and underlie dominant macular dystrophy.Research square · 2026Article
- Tubulin flux at spastin-induced nanodamage sites regulates microtubule rescue frequency and EB1 lifetimes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Insights into retinal disease and non-tubulin glutamylation from a RPGR-TTLL5 complex structure.The Journal of cell biology · 2026Article
- KATANIN promotes cell elongation and division to generate proper cell numbers in maize organs.Nature communications · 2026Article
- Microtubule lattice defects facilitate spastin-mediated severing.Journal of cell science · 2026Article
- Article
- N-terminal phosphorylation inhibits Arabidopsis katanin and affects vegetative and reproductive development in opposite ways.bioRxiv : the preprint server for biology · 2026Article
- PCNA is a nucleotide exchange factor for the clamp loader ATPase complex.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- PCNA is a Nucleotide Exchange Factor for the Clamp Loader ATPase Complex.bioRxiv : the preprint server for biology · 2025Article
- Hydrolysis-dependent severing tunes internal monomeric heterogeneity to shape actin length distributions.bioRxiv : the preprint server for biology · 2025Article
- Constructing an active chimeric pRNA ring with a stoichiometry of six and identifying 12 domains of the pRNA ring binding to the 12-subunit channel of phi29 DNA-packaging motor.RNA (New York, N.Y.) · 2025Article
- Role of Residues Undergoing Hereditary Spastic Paraplegias Mutations: Insights from Simulating the Spiral to Ring Transition in Katanin.Journal of chemical information and modeling · 2025Article
- Alpha-tubulin tails regulate axoneme differentiation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Molecular basis of FIGNL1 in dissociating RAD51 from DNA and chromatin.Science (New York, N.Y.) · 2025Article
- Exploring purine analogues as inhibitors against Katanin, a microtubule severing enzyme using molecular modeling approach.Scientific reports · 2024Article
- Visualization of the Cdc48 AAA+ ATPase protein unfolding pathway.Nature communications · 2024Article
- Molecular basis of FIGNL1 in dissociating RAD51 from DNA and chromatin.bioRxiv : the preprint server for biology · 2024Article
- Epsilon tubulin is an essential determinant of microtubule-based structures in male germ cells.EMBO reports · 2024Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The AAA ATPase katanin severs microtubules. It is critical in cell division, centriole biogenesis, and neuronal morphogenesis. Its mutation causes microcephaly. The microtubule templates katanin hexamerization and activates its ATPase. The structural basis for these activities and how they lead to severing is unknown. Here, we show that β-tubulin tails are necessary and sufficient for severing. Cryoelectron microscopy (cryo-EM) structures reveal the essential tubulin tail glutamates gripped by a double spiral of electropositive loops lining the katanin central pore. Each spiral couples allosterically to the ATPase and binds alternating, successive substrate residues, with consecutive residues coordinated by adjacent protomers. This tightly couples tail binding, hexamerization, and ATPase activation. Hexamer structures in different states suggest an ATPase-driven, ratchet-like translocation of the tubulin tail through the pore. A disordered region outside the AAA core anchors katanin to the microtubule while the AAA motor exerts the forces that extract tubulin dimers and sever the microtubule.
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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.