ArticleeLife2015
The C-terminal region of the motor protein MCAK controls its structure and activity through a conformational switch.
Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers, 1 of them a synthesis that pooled it.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
26 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
- KIF2C condensation concentrates PLK1 and phosphorylated BRCA2 on kinetochore microtubules in mitosis.Nucleic acids research · 2025Article
- Mechanism and regulation of kinesin motors.Nature reviews. Molecular cell biology · 2025Review
- Potent microtubule-depolymerizing activity of a mitotic Kif18b-MCAK-EB network.Journal of cell science · 2023Article
- Article
- A synthetic ancestral kinesin-13 depolymerizes microtubules faster than any natural depolymerizing kinesin.Open biology · 2022Article
- Tension promotes kinetochore-microtubule release by Aurora B kinase.The Journal of cell biology · 2021Article
- MYC Dysregulates Mitosis, Revealing Cancer Vulnerabilities.Cell reports · 2020Article
- In Vitro FRET- and Fluorescence-Based Assays to Study Protein Conformation and Protein-Protein Interactions in Mitosis.Methods in molecular biology (Clifton, N.J.) · 2020Article
- A rapid computational approach identifies SPICE1 as an Aurora kinase substrate.Molecular biology of the cell · 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
- Insights into Kinesin-1 Activation from the Crystal Structure of KLC2 Bound to JIP3.Structure (London, England : 1993) · 2018Article
- Spindle rotation in human cells is reliant on a MARK2-mediated equatorial spindle-centering mechanism.The Journal of cell biology · 2018Article
- The kinetochore-microtubule interface at a glance.Journal of cell science · 2018Review
- Microtubule end tethering of a processive kinesin-8 motor Kif18b is required for spindle positioning.The Journal of cell biology · 2018Article
- A small-molecule activator of kinesin-1 drives remodeling of the microtubule network.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin.Nature communications · 2017Article
- Article
- GTSE1 tunes microtubule stability for chromosome alignment and segregation by inhibiting the microtubule depolymerase MCAK.The Journal of cell biology · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
The precise regulation of microtubule dynamics is essential during cell division. The kinesin-13 motor protein MCAK is a potent microtubule depolymerase. The divergent non-motor regions flanking the ATPase domain are critical in regulating its targeting and activity. However, the molecular basis for the function of the non-motor regions within the context of full-length MCAK is unknown. Here, we determine the structure of MCAK motor domain bound to its regulatory C-terminus. Our analysis reveals that the MCAK C-terminus binds to two motor domains in solution and is displaced allosterically upon microtubule binding, which allows its robust accumulation at microtubule ends. These results demonstrate that MCAK undergoes long-range conformational changes involving its C-terminus during the soluble to microtubule-bound transition and that the C-terminus-motor interaction represents a structural intermediate in the MCAK catalytic cycle. Together, our work reveals intrinsic molecular mechanisms underlying the regulation of kinesin-13 activity.
Indexed as
Identifiers
What OpenQuestion holds
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.