ArticleCurrent biology : CB2009
Tyrosines in the kinesin-5 head domain are necessary for phosphorylation by Wee1 and for mitotic spindle integrity.
Article in Current biology : CB, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 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
- 'Mitotic' kinesin-5 is a dynamic brake for axonal growth in Drosophila.Development (Cambridge, England) · 2025Article
- Genome-Wide Expression Profiling and Phenotypic Analysis of Downstream Targets Identify the Fox Transcription Factor Jumeau as a Master Regulator of Cardiac Progenitor Cell Division.International journal of molecular sciences · 2024Article
- Article
- Phosphoregulation of Kinesins Involved in Long-Range Intracellular Transport.Frontiers in cell and developmental biology · 2022Review
- Mechanisms by Which Kinesin-5 Motors Perform Their Multiple Intracellular Functions.International journal of molecular sciences · 2021Review
- Synthetic-Evolution Reveals Narrow Paths to Regulation of theInternational journal of biological sciences · 2019Article
- Wee1 kinase inhibitor MK-1775 induces apoptosis of acute lymphoblastic leukemia cells and enhances the efficacy of doxorubicin involving downregulation of Notch pathway.Oncology letters · 2018Article
- Src family kinase phosphorylation of the motor domain of the human kinesin-5, Eg5.Cytoskeleton (Hoboken, N.J.) · 2017Article
- Three Cdk1 sites in the kinesin-5 Cin8 catalytic domain coordinate motor localization and activity during anaphase.Cellular and molecular life sciences : CMLS · 2017Article
- Microtubules and Growth Cones: Motors Drive the Turn.Trends in neurosciences · 2016Review
- Budding yeast Swe1 is involved in the control of mitotic spindle elongation and is regulated by Cdc14 phosphatase during mitosis.The Journal of biological chemistry · 2015Article
- Mechanism and regulation of kinesin-5, an essential motor for the mitotic spindle.Biology of the cell · 2014Review
- Inflammatory stress and sarcomagenesis: a vicious interplay.Cell stress & chaperones · 2014Review
- Review
- The dynamic cytoskeleton of the developing male germ cell.Biology of the cell · 2012Review
- MK1775, a selective Wee1 inhibitor, shows single-agent antitumor activity against sarcoma cells.Molecular cancer therapeutics · 2012Article
- WEE1 inhibition sensitizes osteosarcoma to radiotherapy.BMC cancer · 2011Article
- Phospho-regulation of kinesin-5 during anaphase spindle elongation.Journal of cell science · 2011Article
- Drosophila Xpd regulates Cdk7 localization, mitotic kinase activity, spindle dynamics, and chromosome segregation.PLoS genetics · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Mitotic spindle assembly and maintenance relies on kinesin-5 motors that act as bipolar homotetramers to crosslink microtubules. Kinesin-5 motors have been the subject of extensive structure-function analysis, but the regulation of their activity in the context of mitotic progression remains less well understood. We report here that Drosophila kinesin-5 (KLP61F) is regulated by Drosophila Wee1 (dWee1). Wee1 tyrosine kinases are known to regulate mitotic entry via inhibitory phosphorylation of Cdk1. Recently, we showed that dWee1 also plays a role in mitotic spindle positioning through gamma-tubulin and spindle fidelity through an unknown mechanism. Here, we investigated whether a KLP61F-dWee1 interaction could explain the latter role of dWee1. We found that dWee1 phosphorylates KLP61F in vitro on three tyrosines within the head domain, the catalytic region that mediates movement along microtubules. In vivo, KLP61F with tyrosine-->phenylalanine mutations fails to complement a klp61f mutant and dominantly induces spindle defects similar to ones seen in dwee1 mutants. We propose that phosphorylation of the KLP61F catalytic domain by dWee1 is important for the motor's function. This study identifies a second substrate for a Wee1 kinase and provides evidence for phosphoregulation of a kinesin in the head domain.
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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.