ArticleThe Journal of biological chemistry2013
Binding of the CYK-4 subunit of the centralspindlin complex induces a large scale conformational change in the kinesin subunit.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- A key role for centralspindlin and Ect2 in the development of multicellularity and the emergence of Metazoa.Current biology : CB · 2025Article
- Centralspindlin-mediated transport of RhoGEF positions the cleavage plane for cytokinesis.Science signaling · 2023Article
- Article
- Mechanistic insights into central spindle assembly mediated by the centralspindlin complex.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- CYK4 relaxes the bias in the off-axis motion by MKLP1 kinesin-6.Communications biology · 2021Article
- Molecular Mechanism of Cytokinesis.Annual review of biochemistry · 2019Review
- Site-Directed Fluorescence Approaches for Dynamic Structural Biology of Membrane Peptides and Proteins.Frontiers in molecular biosciences · 2019Review
- Temporal regulation of epithelium formation mediated by FoxA, MKLP1, MgcRacGAP, and PAR-6.Molecular biology of the cell · 2017Article
- Tum/RacGAP functions as a switch activating the Pav/kinesin-6 motor.Nature communications · 2016Article
- CYK4 promotes antiparallel microtubule bundling by optimizing MKLP1 neck conformation.PLoS biology · 2015Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Centralspindlin is a critical regulator of cytokinesis in animal cells. It is a tetramer consisting of ZEN-4/MKLP1, a kinesin-6 motor, and CYK-4/MgcRacGAP, a Rho GTPase-activating protein. At anaphase, centralspindlin localizes to a narrow region of antiparallel microtubule overlap and initiates central spindle assembly. Central spindle assembly requires complex formation between ZEN-4 and CYK-4. However, the structural consequences of CYK-4 binding to ZEN-4 are unclear as are the mechanisms of microtubule bundling. Here we investigate whether CYK-4 binding induces a conformational change in ZEN-4. Characterization of the structure and conformational dynamics of the minimal interacting regions between ZEN-4 and CYK-4 by continuous wave EPR and double electron-electron resonance (DEER) spectroscopy reveals that CYK-4 binding dramatically stabilizes the relative positions of the neck linker regions of ZEN-4. Additionally, our data indicate that each neck linker is similarly structured in the bound and unbound states. CYK-4 binding decreases the rate of ZEN-4-mediated microtubule gliding. These results constrain models for the molecular organization of centralspindlin.
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