ArticleProceedings of the National Academy of Sciences of the United States of America2018
A posttranslational modification of the mitotic kinesin Eg5 that enhances its mechanochemical coupling and alters its mitotic function.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- A Phosphorylation Switch Governs KIF11's Mechanical Output During Mitosis.bioRxiv : the preprint server for biology · 2026Article
- Kinesin Spindle Protein (KIF11) in Mitosis and Cancer.International journal of molecular sciences · 2025Review
- Eg5 UFMylation promotes spindle organization during mitosis.Cell death & disease · 2024Article
- KIF11 UFMylation Maintains Photoreceptor Cilium Integrity and Retinal Homeostasis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Mitotic Functions and Characters of KIF11 in Cancers.Biomolecules · 2024Review
- Modification of the neck-linker of KIF18A alters Microtubule subpopulation preference.Molecular biology of the cell · 2024Article
- The phosphorylation and dephosphorylation switch of VCP/p97 regulates the architecture of centrosome and spindle.Cell death and differentiation · 2022Article
- Pathogenic mutations in the chromokinesin KIF22 disrupt anaphase chromosome segregation.eLife · 2022Article
- NAT10 regulates mitotic cell fate by acetylating Eg5 to control bipolar spindle assembly and chromosome segregation.Cell death and differentiation · 2022Article
- A stop or go switch: glycogen synthase kinase 3β phosphorylation of the kinesin 1 motor domain at Ser314 halts motility without detaching from microtubules.Development (Cambridge, England) · 2021Article
- Article
- Mechanisms by Which Kinesin-5 Motors Perform Their Multiple Intracellular Functions.International journal of molecular sciences · 2021Review
- Pathogenic mutations in the kinesin-3 motor KIF1A diminish force generation and movement through allosteric mechanisms.The Journal of cell biology · 2021Article
- Exploration and validation of a novel prognostic signature based on comprehensive bioinformatics analysis in hepatocellular carcinoma.Bioscience reports · 2020Article
- The Role of CHK1 Varies with the Status of Oestrogen-receptor and Progesterone-receptor in the Targeted Therapy for Breast Cancer.International journal of biological sciences · 2020Article
- Article
- The function of histone acetylation in cervical cancer development.Bioscience reports · 2019Review
- Non-canonical functions of the mitotic kinesin Eg5.Thoracic cancer · 2018Review
- Kif15 functions as an active mechanical ratchet.Molecular biology of the cell · 2018Article
Corrections and comments
- Erratum issued
Authors and funding
14 authors at 8 institutions in 1 country.
Funding
Abstract
Numerous posttranslational modifications have been described in kinesins, but their consequences on motor mechanics are largely unknown. We investigated one of these-acetylation of lysine 146 in Eg5-by creating an acetylation mimetic lysine to glutamine substitution (K146Q). Lysine 146 is located in the α2 helix of the motor domain, where it makes an ionic bond with aspartate 91 on the neighboring α1 helix. Molecular dynamics simulations predict that disrupting this bond enhances catalytic site-neck linker coupling. We tested this using structural kinetics and single-molecule mechanics and found that the K146Q mutation increases motor performance under load and coupling of the neck linker to catalytic site. These changes convert Eg5 from a motor that dissociates from the microtubule at low load into one that is more tightly coupled and dissociation resistant-features shared by kinesin 1. These features combined with the increased propensity to stall predict that the K146Q Eg5 acetylation mimetic should act in the cell as a "brake" that slows spindle pole separation, and we have confirmed this by expressing this modified motor in mitotically active cells. Thus, our results illustrate how a posttranslational modification of a kinesin can be used to fine tune motor behavior to meet specific physiological needs.
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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.