ArticleJournal of molecular biology2013
N-terminal phosphorylation of p60 katanin directly regulates microtubule severing.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 43 citations in OpenAlex.
- N-terminal phosphorylation inhibits Arabidopsis katanin and affects vegetative and reproductive development in opposite ways.bioRxiv : the preprint server for biology · 2026Article
- A Tale of 12 Tails: Katanin Severing Activity Affected by Carboxy-Terminal Tail Sequences.Biomolecules · 2023Article
- The Mammalian Family of Katanin Microtubule-Severing Enzymes.Frontiers in cell and developmental biology · 2021Review
- Spastin recovery in hereditary spastic paraplegia by preventing neddylation-dependent degradation.Life science alliance · 2020Article
- Katanin P60: a potential biomarker for lymph node metastasis and prognosis for non-small cell lung cancer.World journal of surgical oncology · 2020Article
- Phosphorylation of the microtubule-severing AAA+ enzyme Katanin regulates C. elegans embryo development.The Journal of cell biology · 2020Article
- Katanin Grips the β-Tubulin Tail through an Electropositive Double Spiral to Sever Microtubules.Developmental cell · 2020Article
- Article
- Phosphorylation of Plant Microtubule-Associated Proteins During Cell Division.Frontiers in plant science · 2019Review
- Microtubule-severing enzymes: From cellular functions to molecular mechanism.The Journal of cell biology · 2018Review
- Creation and testing of a new, local microtubule-disruption tool based on the microtubule-severing enzyme, katanin p60.Cytoskeleton (Hoboken, N.J.) · 2018Article
- Understanding eukaryotic chromosome segregation from a comparative biology perspective.Journal of cell science · 2018Review
- The role of katanin p60 in breast cancer bone metastasis.Oncology letters · 2018Article
- Katanin spiral and ring structures shed light on power stroke for microtubule severing.Nature structural & molecular biology · 2017Article
- Proteomic Analysis of the Mammalian Katanin Family of Microtubule-severing Enzymes Defines Katanin p80 subunit B-like 1 (KATNBL1) as a Regulator of Mammalian Katanin Microtubule-severing.Molecular & cellular proteomics : MCP · 2016Article
- A novel family of katanin-like 2 protein isoforms (KATNAL2), interacting with nucleotide-binding proteins Nubp1 and Nubp2, are key regulators of different MT-based processes in mammalian cells.Cellular and molecular life sciences : CMLS · 2016Article
- Katanin Severing and Binding Microtubules Are Inhibited by Tubulin Carboxy Tails.Biophysical journal · 2015Article
- Kif2a depletion generates chromosome segregation and pole coalescence defects in animal caps and inhibits gastrulation of the Xenopus embryo.Molecular biology of the cell · 2015Article
- The non-catalytic domains of Drosophila katanin regulate its abundance and microtubule-disassembly activity.PloS one · 2015Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Proteins of the AAA (ATPases associated with various cellular activities) family often have complex modes of regulation due to their central position in important cellular processes. p60 katanin, an AAA protein that severs and depolymerizes microtubules, is subject to multiple modes of regulation including a phosphorylation in the N-terminal domain involved in mitotic control of severing. Phosphorylation decreases severing activity in Xenopus egg extracts and is involved in controlling spindle length. Here, we show that the evolutionarily divergent N-terminal domains of p60 have maintained hotspots of mitotic kinase regulation. By reconstituting in vitro severing reactions, we show that phosphomimetic modification at amino acid position 131 in Xenopus laevis p60 decreases severing and microtubule-stimulated ATPase activity without affecting the binding affinity of p60 for microtubules. At high concentrations of the phosphomimetic mutant p60, wild-type levels of activity could be observed, indicating a more switch-like threshold of activity that is controlled by regulating oligomerization on the microtubule. This provides a cellular mechanism for high local concentrations of p60, like those found on spindle poles, to maintain severing activity while most of the protein is inhibited. Overall, we have shown that the modular domain architecture of AAA proteins allows for precise control of cellular activities with simple modifications.
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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.