ArticleThe Journal of biological chemistry2015
New Insights into the Coupling between Microtubule Depolymerization and ATP Hydrolysis by Kinesin-13 Protein Kif2C.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.
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Who cites it
18 citing papers in PubMed, 1 synthesis or guideline pooled it, 34 citations in OpenAlex.
- 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
- Article
- Human endogenous retrovirus ERVK3-1 characterizes a metabolically active and immunosuppressive subtype of liver cancer.Virology journal · 2025Article
- Functional genetics reveals modulators of antimicrotubule drug sensitivity.The Journal of cell biology · 2025Article
- Modeling study of kinesin-13 MCAK microtubule depolymerase.European biophysics journal : EBJ · 2024Article
- Functional genetics reveals modulators of anti-microtubule drug sensitivity.bioRxiv : the preprint server for biology · 2024Article
- Article
- Mechanochemical tuning of a kinesin motor essential for malaria parasite transmission.Nature communications · 2022Article
- Kinesin-8-specific loop-2 controls the dual activities of the motor domain according to tubulin protofilament shape.Nature communications · 2022Article
- KIF2C regulates synaptic plasticity and cognition in mice through dynamic microtubule depolymerization.eLife · 2022Article
- KIF2C promotes the proliferation of hepatocellular carcinoma cellsExperimental and therapeutic medicine · 2021Article
- These motors were made for walking.Protein science : a publication of the Protein Society · 2020Review
- The depolymerase activity of MCAK shows a graded response to Aurora B kinase phosphorylation through allosteric regulation.Journal of cell science · 2019Article
- 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
- Microarray Expression Profile of lncRNAs and mRNAs in Rats with Traumatic Brain Injury after A2B5+ Cell Transplantation.Cell transplantation · 2017Article
- Insight into microtubule disassembly by kinesin-13s from the structure of Kif2C bound to tubulin.Nature communications · 2017Article
- Review: Mechanochemistry of the kinesin-1 ATPase.Biopolymers · 2016Review
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Kinesin-13 proteins depolymerize microtubules in an ATP hydrolysis-dependent manner. The coupling between these two activities remains unclear. Here, we first studied the role of the kinesin-13 subfamily-specific loop 2 and of the KVD motif at the tip of this loop. Shortening the loop, the lysine/glutamate interchange and the additional Val to Ser substitution all led to Kif2C mutants with decreased microtubule-stimulated ATPase and impaired depolymerization capability. We rationalized these results based on a structural model of the Kif2C-ATP-tubulin complex derived from the recently determined structures of kinesin-1 bound to tubulin. In this model, upon microtubule binding Kif2C undergoes a conformational change governed in part by the interaction of the KVD motif with the tubulin interdimer interface. Second, we mutated to an alanine the conserved glutamate residue of the switch 2 nucleotide binding motif. This mutation blocks motile kinesins in a post-conformational change state and inhibits ATP hydrolysis. This Kif2C mutant still depolymerized microtubules and yielded complexes of one Kif2C with two tubulin heterodimers. These results demonstrate that the structural change of Kif2C-ATP upon binding to microtubule ends is sufficient for tubulin release, whereas ATP hydrolysis is not required. Overall, our data suggest that the conformation reached by kinesin-13s upon tubulin binding is similar to that of tubulin-bound, ATP-bound, motile kinesins but that this conformation is adapted to microtubule depolymerization.
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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.