ArticleThe Journal of cell biology2024
Microtubule-binding domains in Katanin p80 subunit are essential for severing activity in C. elegans.
Article in The Journal of cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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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.
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Who cites it
4 citing papers in PubMed, 6 citations in OpenAlex.
- Differential contributions of β-tubulin isotypes to acentrosomal oocyte meiosis inbioRxiv : the preprint server for biology · 2025Article
- Fidgetin binds spastin to attenuate the microtubule-severing activity.Biochimica et biophysica acta. Molecular cell research · 2025Article
- Roles of Tubulin Concentration during Prometaphase and Ran-GTP during Anaphase ofLife science alliance · 2024Article
- Roles of Tubulin Concentration during Prometaphase and Ran-GTP during Anaphase ofbioRxiv : the preprint server for biology · 2024Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Microtubule-severing enzymes (MSEs), such as Katanin, Spastin, and Fidgetin play essential roles in cell division and neurogenesis. They damage the microtubule (MT) lattice, which can either destroy or amplify the MT cytoskeleton, depending on the cellular context. However, little is known about how they interact with their substrates. We have identified the microtubule-binding domains (MTBD) required for Katanin function in C. elegans. Katanin is a heterohexamer of dimers containing a catalytic subunit p60 and a regulatory subunit p80, both of which are essential for female meiotic spindle assembly. Here, we report that p80-like(MEI-2) dictates Katanin binding to MTs via two MTBDs composed of basic patches. Substituting these patches reduces Katanin binding to MTs, compromising its function in female meiotic-spindle assembly. Structural alignments of p80-like(MEI-2) with p80s from different species revealed that the MTBDs are evolutionarily conserved, even if the specific amino acids involved vary. Our findings highlight the critical importance of the regulatory subunit (p80) in providing MT binding to the Katanin complex.
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Registered trials
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