ArticleCell2007
Vik1 modulates microtubule-Kar3 interactions through a motor domain that lacks an active site.
Article in Cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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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.
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Who cites it
51 citing papers in PubMed.
- Mutation of OsKIF14.3, a Kinesin-14 Subfamily Protein, Altered Starch Metabolism and Caused Yellowish Leaf in Rice.International journal of molecular sciences · 2025Article
- A coordinated kinase and phosphatase network regulates Stu2 recruitment to yeast kinetochores.The Journal of cell biology · 2025Article
- Design of allosteric sites into rotary motor VNature chemistry · 2023Article
- Cik1 and Vik1 accessory proteins confer distinct functions to the kinesin-14 Kar3.Journal of cell science · 2023Article
- Modeling processive motion of kinesin-13 MCAK and kinesin-14 Cik1-Kar3 molecular motors.Protein science : a publication of the Protein Society · 2021Article
- The EB1-Kinesin-14 complex is required for efficient metaphase spindle assembly and kinetochore bi-orientation.The Journal of cell biology · 2020Article
- Inclusion Formation and Toxicity of the ALS Protein RGNEF and Its Association with the Microtubule Network.International journal of molecular sciences · 2020Article
- Small molecule allosteric uncoupling of microtubule depolymerase activity from motility in human Kinesin-5 during mitotic spindle assembly.Scientific reports · 2019Article
- Article
- Interrogation of γ-tubulin alleles using high-resolution fitness measurements reveals a distinct cytoplasmic function in spindle alignment.Scientific reports · 2017Article
- The Aspergillus nidulans bimC4 mutation provides an excellent tool for identification of kinesin-14 inhibitors.Fungal genetics and biology : FG & B · 2015Article
- Kinesin Motor Enzymology: Chemistry, Structure, and Physics of Nanoscale Molecular Machines.Biophysical reviews · 2015Article
- Candida albicans Kinesin Kar3 Depends on a Cik1-Like Regulatory Partner Protein for Its Roles in Mating, Cell Morphogenesis, and Bipolar Spindle Formation.Eukaryotic cell · 2015Article
- Drosophila Ncd reveals an evolutionarily conserved powerstroke mechanism for homodimeric and heterodimeric kinesin-14s.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Article
- Minus-end-directed Kinesin-14 motors align antiparallel microtubules to control metaphase spindle length.Developmental cell · 2014Article
- Prime movers: the mechanochemistry of mitotic kinesins.Nature reviews. Molecular cell biology · 2014Review
- Kar3Vik1 mechanochemistry is inhibited by mutation or deletion of the C terminus of the Vik1 subunit.The Journal of biological chemistry · 2013Article
- Common mechanistic themes for the powerstroke of kinesin-14 motors.Journal of structural biology · 2013Article
- The molecular basis for kinesin functional specificity during mitosis.Cytoskeleton (Hoboken, N.J.) · 2013Review
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4 authors.
Funding
Abstract
Conventional kinesin and class V and VI myosins coordinate the mechanochemical cycles of their motor domains for processive movement of cargo along microtubules or actin filaments. It is widely accepted that this coordination is achieved by allosteric communication or mechanical strain between the motor domains, which controls the nucleotide state and interaction with microtubules or actin. However, questions remain about the interplay between the strain and the nucleotide state. We present an analysis of Saccharomyces cerevisiae Kar3/Vik1, a heterodimeric C-terminal Kinesin-14 containing catalytic Kar3 and the nonmotor protein Vik1. The X-ray crystal structure of Vik1 exhibits a similar fold to the kinesin and myosin catalytic head, but lacks an ATP binding site. Vik1 binds more tightly to microtubules than Kar3 and facilitates cooperative microtubule decoration by Kar3/Vik1 heterodimers, and yet allows motility. These results demand communication between Vik1 and Kar3 via a mechanism that coordinates their interactions with microtubules.
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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.