ArticleOpen biology2016
The family-specific α4-helix of the kinesin-13, MCAK, is critical to microtubule end recognition.
Article in Open biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Article
- Mechanism of spindle stability and poleward flux regulating spindle length during the metaphase.iScience · 2025Article
- FGF-Mediated Axon Guidance: Role of Downstream Signaling Pathways in Cytoskeletal Control.Cells · 2025Review
- Modeling study of kinesin-13 MCAK microtubule depolymerase.European biophysics journal : EBJ · 2024Article
- A synthetic ancestral kinesin-13 depolymerizes microtubules faster than any natural depolymerizing kinesin.Open biology · 2022Article
- Article
- Identification of key residues that regulate the interaction of kinesins with microtubule ends.Cytoskeleton (Hoboken, N.J.) · 2019Article
- The depolymerase activity of MCAK shows a graded response to Aurora B kinase phosphorylation through allosteric regulation.Journal of cell science · 2019Article
- Parts list for a microtubule depolymerising kinesin.Biochemical Society transactions · 2018Review
- Altered chemomechanical coupling causes impaired motility of the kinesin-4 motors KIF27 and KIF7.The Journal of cell biology · 2018Article
- Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin.Nature communications · 2017Article
- Article
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Authors and funding
6 authors.
Funding
Abstract
Kinesins that influence the dynamics of microtubule growth and shrinkage require the ability to distinguish between the microtubule end and the microtubule lattice. The microtubule depolymerizing kinesin MCAK has been shown to specifically recognize the microtubule end. This ability is key to the action of MCAK in regulating microtubule dynamics. We show that the α4-helix of the motor domain is crucial to microtubule end recognition. Mutation of the residues K524, E525 and R528, which are located in the C-terminal half of the α4-helix, specifically disrupts the ability of MCAK to recognize the microtubule end. Mutation of these residues, which are conserved in the kinesin-13 family and discriminate members of this family from translocating kinesins, impairs the ability of MCAK to discriminate between the microtubule lattice and the microtubule end.
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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.