ArticleBiophysical journal2015
Katanin Severing and Binding Microtubules Are Inhibited by Tubulin Carboxy Tails.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.
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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
33 citing papers in PubMed, 1 synthesis or guideline pooled it, 60 citations in OpenAlex.
- [Prognostic Value of STMN1 Expression in Non-small Cell Lung Cancer: A Meta-analysis].Zhongguo fei ai za zhi = Chinese journal of lung cancer · 2024Pooled it
- Molecular Insights Into the Differential Binding Affinity of Human Katanin Hexamer for C-Terminal Tails of β-Tubulin Isotypes.Cytoskeleton (Hoboken, N.J.) · 2026Article
- Microtubule-binding domains in Katanin p80 subunit are essential for severing activity in C. elegans.The Journal of cell biology · 2024Article
- Article
- STMN1 Promotes Tumor Metastasis in Non-small Cell Lung Cancer Through Microtubule-dependent And Nonmicrotubule-dependent Pathways.International journal of biological sciences · 2024Article
- The minus-end depolymerase KIF2A drives flux-like treadmilling of γTuRC-uncapped microtubules.The Journal of cell biology · 2023Article
- Lateral and longitudinal compaction of PRC1 overlap zones drives stabilization of interzonal microtubules.Molecular biology of the cell · 2023Article
- A Tale of 12 Tails: Katanin Severing Activity Affected by Carboxy-Terminal Tail Sequences.Biomolecules · 2023Article
- Deciphering the Tubulin Language: Molecular Determinants and Readout Mechanisms of the Tubulin Code in Neurons.International journal of molecular sciences · 2023Review
- Combinatorial and antagonistic effects of tubulin glutamylation and glycylation on katanin microtubule severing.Developmental cell · 2022Article
- In Vitro Reconstitution of Microtubule Dynamics and Severing Imaged by Label-Free Interference-Reflection Microscopy.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Factors underlying asymmetric pore dynamics of disaggregase and microtubule-severing AAA+ machines.Biophysical journal · 2021Article
- Micron-scale geometrical features of microtubules as regulators of microtubule organization.eLife · 2021Review
- Impact of the 'tubulin economy' on the formation and function of the microtubule cytoskeleton.Current opinion in cell biology · 2021Review
- The Mammalian Family of Katanin Microtubule-Severing Enzymes.Frontiers in cell and developmental biology · 2021Review
- Protein Diffusion on Charged Biopolymers: DNA versus Microtubule.Biophysical journal · 2020Article
- Tubulin tails and their modifications regulate protein diffusion on microtubules.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Stathmin Regulates Spatiotemporal Variation in the Memory Loop in Single-Prolonged Stress Rats.Journal of molecular neuroscience : MN · 2020Article
- RhoA-GTPase Modulates Neurite Outgrowth by Regulating the Expression of Spastin and p60-Katanin.Cells · 2020Article
- Katanin Grips the β-Tubulin Tail through an Electropositive Double Spiral to Sever Microtubules.Developmental cell · 2020Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Microtubule dynamics in cells are regulated by associated proteins that can be either stabilizers or destabilizers. A class of destabilizers that is important in a large number of cellular activities is the microtubule-severing enzymes, yet little is known about how they function. Katanin p60 was the first ATPase associated with microtubule severing. Here, we investigate the activity of katanin severing using a GFP-labeled human version. We quantify the effect of katanin concentration on katanin binding and severing activity. We find that free tubulin can inhibit severing activity by interfering with katanin binding to microtubules. The inhibition is mediated by the sequence of the tubulin and specifically depends on the carboxy-terminal tails. We directly investigate the inhibition effect of tubulin carboxy-terminal tails using peptide sequences of α-, β-, or detyrosinated α-tubulin tails that have been covalently linked to bovine serum albumin. Our results show that β-tubulin tails are the most effective at inhibiting severing, and that detyrosinated α-tubulin tails are the least effective. These results are distinct from those for other severing enzymes and suggest a scheme for regulation of katanin activity in cells dependent on free tubulin concentration and the modification state of the tubulin.
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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.