ArticleMolecular biology of the cell2006
Full-length dimeric MCAK is a more efficient microtubule depolymerase than minimal domain monomeric MCAK.
Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers, 1 of them a synthesis that pooled it.
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Who cites it
47 citing papers in PubMed, 1 synthesis or guideline pooled it.
- KIF2C/MCAK a prognostic biomarker and its oncogenic potential in malignant progression, and prognosis of cancer patients: a systematic review and meta-analysis as biomarker.Critical reviews in clinical laboratory sciences · 2024Pooled it
- Microtubules guide Aurora B substrate geometries for accurate chromosome segregation.Science advances · 2026Article
- The Kinesin-14 tail: Dual microtubule binding domains drive spindle morphogenesis through tight microtubule cross-linking and robust sliding.Molecular biology of the cell · 2025Article
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Modeling study of kinesin-13 MCAK microtubule depolymerase.European biophysics journal : EBJ · 2024Article
- Cep104 is a component of the centriole distal tip complex that regulates centriole growth and contributes to Drosophila spermiogenesis.Current biology : CB · 2023Article
- Structural basis of microtubule depolymerization by the kinesin-like activity of HIV-1 Rev.Structure (London, England : 1993) · 2023Article
- The minus-end depolymerase KIF2A drives flux-like treadmilling of γTuRC-uncapped microtubules.The Journal of cell biology · 2023Article
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- Importin α/β promote Kif18B microtubule association and enhance microtubule destabilization activity.Molecular biology of the cell · 2023Article
- Article
- A synthetic ancestral kinesin-13 depolymerizes microtubules faster than any natural depolymerizing kinesin.Open biology · 2022Article
- UNC-45A breaks the microtubule lattice independently of its effects on non-muscle myosin II.Journal of cell science · 2021Article
- Conditional switching of KIF2A mutation provides new insights into cortical malformation pathogeny.Human molecular genetics · 2020Article
- Kinesin-13 and Kinesin-8 Function during Cell Growth and Division in the MossThe Plant cell · 2020Article
- Interplay between the Kinesin and Tubulin Mechanochemical Cycles Underlies Microtubule Tip Tracking by the Non-motile Ciliary Kinesin Kif7.Developmental cell · 2019Article
- Parts list for a microtubule depolymerising kinesin.Biochemical Society transactions · 2018Review
- Ternary complex of Kif2A-bound tandem tubulin heterodimers represents a kinesin-13-mediated microtubule depolymerization reaction intermediate.Nature communications · 2018Article
- Cryo-EM reveals the structural basis of microtubule depolymerization by kinesin-13s.Nature communications · 2018Article
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Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
MCAK belongs to the Kinesin-13 family, whose members depolymerize microtubules rather than translocate along them. We defined the minimal functional unit of MCAK as the catalytic domain plus the class specific neck (MD-MCAK), which is consistent with previous reports. We used steady-state ATPase kinetics, microtubule depolymerization assays, and microtubule.MCAK cosedimentation assays to compare the activity of full-length MCAK, which is a dimer, with MD-MCAK, which is a monomer. Full-length MCAK exhibits higher ATPase activity, more efficient microtubule end binding, and reduced affinity for the tubulin heterodimer. Our studies suggest that MCAK dimerization is important for its catalytic cycle by promoting MCAK binding to microtubule ends, enhancing the ability of MCAK to recycle for multiple rounds of microtubule depolymerization, and preventing MCAK from being sequestered by tubulin heterodimers.
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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.