ArticleMolecular & cellular proteomics : MCP2010
Quantitative site-specific phosphorylation dynamics of human protein kinases during mitotic progression.
Article in Molecular & cellular proteomics : MCP, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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26 citing papers in PubMed, 54 citations in OpenAlex.
- Phosphoregulation of interleukin-1 receptor-associated kinase 1 in inflammatory signaling.Frontiers in immunology · 2026Review
- Evaluating cell cycle- and autophagy-associated cellular accumulation of lipid-based nanoparticles.Nature communications · 2025Article
- Identification of PP2A-B55 targets uncovers regulation of emerin during nuclear envelope reassembly inOpen biology · 2023Article
- Systems-level analyses of protein-protein interaction network dysfunctions via epichaperomics identify cancer-specific mechanisms of stress adaptation.Nature communications · 2023Article
- Revisiting degron motifs in human AURKA required for its targeting by APC/CLife science alliance · 2023Article
- Writing and Erasing O-GlcNAc on Casein Kinase 2 Alpha Alters the Phosphoproteome.ACS chemical biology · 2022Article
- Cell Cycle Progression and Synchronization: An Overview.Methods in molecular biology (Clifton, N.J.) · 2022Review
- Cytotoxic, analgesic and anti-inflammatory activity of colchicine and its C-10 sulfur containing derivatives.Scientific reports · 2021Article
- Kinobead/LC-MS Phosphokinome Profiling Enables Rapid Analyses of Kinase-Dependent Cell Signaling Networks.Journal of proteome research · 2020Article
- Cyclin-dependent kinase 1-mediated AMPK phosphorylation regulates chromosome alignment and mitotic progression.Journal of cell science · 2019Article
- A rapid computational approach identifies SPICE1 as an Aurora kinase substrate.Molecular biology of the cell · 2019Article
- Post-translational modifications at the ATP-positioning G-loop that regulate protein kinase activity.Pharmacological research · 2018Review
- Reversible phosphorylation of the 26S proteasome.Protein & cell · 2017Review
- Osmoregulation in the Halophilic Bacterium Halomonas elongata: A Case Study for Integrative Systems Biology.PloS one · 2017Article
- Ubiquitin-Mediated Degradation of Aurora Kinases.Frontiers in oncology · 2015Review
- Greatwall-phosphorylated Endosulfine is both an inhibitor and a substrate of PP2A-B55 heterotrimers.eLife · 2014Article
- The Aurora B kinase in Trypanosoma brucei undergoes post-translational modifications and is targeted to various subcellular locations through binding to TbCPC1.Molecular microbiology · 2014Article
- Cell cycle-dependent phosphorylation of Theileria annulata schizont surface proteins.PloS one · 2014Article
- Ubiquitination site preferences in anaphase promoting complex/cyclosome (APC/C) substrates.Open biology · 2013Article
- A hexylchloride-based catch-and-release system for chemical proteomic applications.ACS chemical biology · 2013Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Reversible protein phosphorylation is a key regulatory mechanism of mitotic progression. Importantly, protein kinases themselves are also regulated by phosphorylation-dephosphorylation processes; hence, phosphorylation dynamics of kinases hold a wealth of information about phosphorylation networks. Here, we investigated the site-specific phosphorylation dynamics of human kinases during mitosis using synchronization of HeLa suspension cells, kinase enrichment, and high resolution mass spectrometry. In biological triplicate analyses, we identified 206 protein kinases and more than 900 protein kinase phosphorylation sites, including 61 phosphorylation sites on activation segments, and quantified their relative abundances across three specific mitotic stages. Around 25% of the kinase phosphorylation site ratios were found to be changed by at least 50% during mitotic progression. Further network analysis of jointly regulated kinase groups suggested that Cyclin-dependent kinase- and mitogen-activated kinase-centered interaction networks are coordinately down- and up-regulated in late mitosis, respectively. Importantly, our data cover most of the already known mitotic kinases and, moreover, identify attractive candidates for future studies of phosphorylation-based mitotic signaling. Thus, the results of this study provide a valuable resource for cell biologists and provide insight into the system properties of the mitotic phosphokinome.
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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.