ArticleProceedings of the National Academy of Sciences of the United States of America2014
Method for identifying phosphorylated substrates of specific cyclin/cyclin-dependent kinase complexes.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
20 citing papers in PubMed, 32 citations in OpenAlex.
- Pools of Independently Cycling Inositol Phosphates Revealed by Pulse Labeling withJournal of the American Chemical Society · 2025Article
- Qualitative rather than quantitative phosphoregulation shapes the end of meiosis I in budding yeast.The EMBO journal · 2024Article
- The diverging role of CDC14B: from mitotic exit in yeast to cell fate control in humans.The EMBO journal · 2023Review
- Phosphoproteomic Approaches for Identifying Phosphatase and Kinase Substrates.Molecules (Basel, Switzerland) · 2023Review
- Cdc14 phosphatase contributes to cell wall integrity and pathogenesis inFrontiers in microbiology · 2023Article
- Stable Isotope Phosphate Labelling of Diverse Metabolites is Enabled by a Family ofAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
- Stable Isotope Phosphate Labelling of Diverse Metabolites is Enabled by a Family ofAngewandte Chemie (International ed. in English) · 2022Article
- Article
- Phosphoregulation of the oncogenic protein regulator of cytokinesis 1 (PRC1) by the atypical CDK16/CCNY complex.Experimental & molecular medicine · 2019Article
- Biochemical analyses reveal amino acid residues critical for cell cycle-dependent phosphorylation of human Cdc14A phosphatase by cyclin-dependent kinase 1.Scientific reports · 2018Article
- A phosphorylation switch turns a positive regulator of phototropism into an inhibitor of the process.Nature communications · 2018Article
- Review
- Machine Learning of Global Phosphoproteomic Profiles Enables Discrimination of Direct versus Indirect Kinase Substrates.Molecular & cellular proteomics : MCP · 2017Article
- Quantitative investigation of human cell surfaceChemical science · 2017Article
- Identifying Kinase Substrates via a Heavy ATP Kinase Assay and Quantitative Mass Spectrometry.Scientific reports · 2016Article
- Cyclin-Dependent Kinase Co-Ordinates Carbohydrate Metabolism and Cell Cycle in S. cerevisiae.Molecular cell · 2016Article
- Phosphoproteome dynamics of Saccharomyces cerevisiae under heat shock and cold stress.Molecular systems biology · 2015Article
- A high-sensitivity phospho-switch triggered by Cdk1 governs chromosome morphogenesis during cell division.Genes & development · 2015Article
- How the cell cycle impacts chromatin architecture and influences cell fate.Frontiers in genetics · 2015Article
- Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
In eukaryotes, cell cycle progression is controlled by cyclin/cyclin-dependent kinase (CDK) pairs. To better understand the details of this process, it is necessary to dissect the CDK's substrate pool in a cyclin- and cell cycle stage-specific way. Here, we report a mass spectrometry-based method that couples rapid isolation of native kinase-substrate complexes to on-bead phosphorylation with heavy-labeled ATP (ATP-γ-(18)O4). This combined in vivo/in vitro method was developed for identifying cyclin/CDK substrates together with their sites of phosphorylation. We used the method to identify Clb5 (S-cyclin)/Cdc28 and Cln2 (G1/S-cyclin)/Cdc28 substrates during S phase in Saccharomyces cerevisiae (Cdc28 is the master CDK in budding yeast). During the work, we discovered that Clb5/Cdc28 specifically phosphorylates S429 in the disordered tail of Cdc14, an essential phosphatase antagonist of Cdc28. This phosphorylation severely decreases the activity of Cdc14, providing a means for modulating the balance of CDK and phosphatase activity.
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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.