ArticleMolecular & cellular proteomics : MCP2013
Identification of direct tyrosine kinase substrates based on protein kinase assay-linked phosphoproteomics.
Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 36 citations in OpenAlex.
- SuFEx chemistry for nucleosides, nucleotides, and nucleic acids.RSC chemical biology · 2026Review
- Aminopeptidase N/CD13 Crosslinking Promotes the Activation and Membrane Expression of Integrin CD11b/CD18.Biomolecules · 2023Article
- Phosphoproteomic Approaches for Identifying Phosphatase and Kinase Substrates.Molecules (Basel, Switzerland) · 2023Review
- Novel Bruton's Tyrosine Kinase (BTK) Substrates for Time-Resolved Luminescence Assays.ACS chemical biology · 2022Article
- Motif-centric phosphoproteomics to target kinase-mediated signaling pathways.Cell reports methods · 2022Article
- Integrated Phosphoproteomics for Identifying Substrates of Human Protein Kinase A (Journal of proteome research · 2021Article
- Comparison of SYK Signaling Networks Reveals the Potential Molecular Determinants of Its Tumor-Promoting and Suppressing Functions.Biomolecules · 2021Article
- Syk-MyD88 Axis Is a Critical Determinant of Inflammatory-Response in Activated Macrophages.Frontiers in immunology · 2021Article
- Reconstructing kinase network topologies from phosphoproteomics data reveals cancer-associated rewiring.Nature biotechnology · 2020Article
- Quantitative phosphoproteomic analysis identifies the potential therapeutic target EphA2 for overcoming sorafenib resistance in hepatocellular carcinoma cells.Experimental & molecular medicine · 2020Article
- Article
- Phosphoproteomics Analysis Identifies Novel Candidate Substrates of the Nonreceptor Tyrosine Kinase,Molecular & cellular proteomics : MCP · 2018Article
- Review
- Determinants of Macromolecular Specificity from Proteomics-Derived Peptide Substrate Data.Current protein & peptide science · 2017Review
- Targeting Syk in Autoimmune Rheumatic Diseases.Frontiers in immunology · 2016Review
- Inhibition of Spleen Tyrosine Kinase Potentiates Paclitaxel-Induced Cytotoxicity in Ovarian Cancer Cells by Stabilizing Microtubules.Cancer cell · 2015Article
- Protein networks and activation of lymphocytes.Current opinion in immunology · 2015Review
- Recent findings and technological advances in phosphoproteomics for cells and tissues.Expert review of proteomics · 2015Review
- Analytical challenges translating mass spectrometry-based phosphoproteomics from discovery to clinical applications.Electrophoresis · 2014Review
- Identification of extracellular signal-regulated kinase 1 (ERK1) direct substrates using stable isotope labeled kinase assay-linked phosphoproteomics.Molecular & cellular proteomics : MCP · 2014Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Protein kinases are implicated in multiple diseases such as cancer, diabetes, cardiovascular diseases, and central nervous system disorders. Identification of kinase substrates is critical to dissecting signaling pathways and to understanding disease pathologies. However, methods and techniques used to identify bona fide kinase substrates have remained elusive. Here we describe a proteomic strategy suitable for identifying kinase specificity and direct substrates in high throughput. This approach includes an in vitro kinase assay-based substrate screening and an endogenous kinase dependent phosphorylation profiling. In the in vitro kinase reaction route, a pool of formerly phosphorylated proteins is directly extracted from whole cell extracts, dephosphorylated by phosphatase treatment, after which the kinase of interest is added. Quantitative proteomics identifies the rephosphorylated proteins as direct substrates in vitro. In parallel, the in vivo quantitative phosphoproteomics is performed in which cells are treated with or without the kinase inhibitor. Together, proteins phosphorylated in vitro overlapping with the kinase-dependent phosphoproteome in vivo represents the physiological direct substrates in high confidence. The protein kinase assay-linked phosphoproteomics was applied to identify 25 candidate substrates of the protein-tyrosine kinase SYK, including a number of known substrates and many novel substrates in human B cells. These shed light on possible new roles for SYK in multiple important signaling pathways. The results demonstrate that this integrated proteomic approach can provide an efficient strategy to screen direct substrates for protein tyrosine kinases.
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