ArticleScientific reports2017
Structural basis of katanin p60:p80 complex formation.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 26 citations in OpenAlex.
- Missense variants in KATNA1 alter microtubule dynamics and underlie dominant macular dystrophy.Research square · 2026Article
- Microtubule-binding domains in Katanin p80 subunit are essential for severing activity in C. elegans.The Journal of cell biology · 2024Article
- Tubulin polyglutamylation differentially regulates microtubule-interacting proteins.The EMBO journal · 2023Article
- Crystal structure of the C-terminal domain of the plant-specific microtubule-associated protein Spiral2.Acta crystallographica. Section F, Structural biology communications · 2023Article
- Crystal structure of the Arabidopsis SPIRAL2 C-terminal domain reveals a p80-Katanin-like domain.PloS one · 2023Article
- Axonal transport deficits in the pathogenesis of diabetic peripheral neuropathy.Frontiers in endocrinology · 2023Review
- Combinatorial and antagonistic effects of tubulin glutamylation and glycylation on katanin microtubule severing.Developmental cell · 2022Article
- Article
- 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
- The Mammalian Family of Katanin Microtubule-Severing Enzymes.Frontiers in cell and developmental biology · 2021Review
- Katanin P60 and P80 in papillary thyroid carcinoma patients: Indicators for exacerbated tumor features and worse disease-free survival.Journal of clinical laboratory analysis · 2020Article
- Review
- Katanin Grips the β-Tubulin Tail through an Electropositive Double Spiral to Sever Microtubules.Developmental cell · 2020Article
- Microtubule-severing enzymes: From cellular functions to molecular mechanism.The Journal of cell biology · 2018Review
- Katanin P80 expression correlates with lymph node metastasis and worse overall survival in patients with breast cancer.Cancer biomarkers : section A of Disease markers · 2018Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
Abstract
Interactions between microtubule (MT) interacting and trafficking (MIT) domains and their binding proteins are important for the accurate progression of many cellular processes that require the AAA+ ATPase machinery. Therefore, knowledge on the structural basis of MIT domain interactions is crucial for understanding the molecular mechanisms underlying AAA+ ATPase function. Katanin is a MT-severing AAA+ ATPase that consists of p60 and p80 subunits. Although, the hexameric p60 subunit is active alone, its association with the p80 subunit greatly enhances both the MT-binding and -severing activities of katanin. However, the molecular mechanism of how the p80 subunit contributes to katanin function is currently unknown. Here, we structurally and functionally characterized the interaction between the two katanin subunits that is mediated by the p60-MIT domain and the p80 C-terminal domain (p80-CTD). We show that p60-MIT and p80-CTD form a tight heterodimeric complex, whose high-resolution structure we determined by X-ray crystallography. Based on the crystal structure, we identified two conserved charged residues that are important for p60-MIT:p80-CTD complex formation and katanin function. Moreover, p60-MIT was compared with other MIT domain structures and similarities are discussed.
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