ArticleMolecular & cellular proteomics : MCP2013
Interrogating cAMP-dependent kinase signaling in Jurkat T cells via a protein kinase A targeted immune-precipitation phosphoproteomics approach.
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 26 papers.
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Who cites it
26 citing papers in PubMed, 50 citations in OpenAlex.
- IKAROS: from chromatin organization to transcriptional elongation control.Cell death and differentiation · 2025Review
- Phosphorylation regulates the chromatin remodeler SMARCAD1 in nucleosome binding, ATP hydrolysis, and histone exchange.The Journal of biological chemistry · 2024Article
- The focal adhesion protein talin is a mechanically gated A-kinase anchoring protein.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- G9a Inhibition Promotes Neuroprotection through GMFB Regulation in Alzheimer's Disease.Aging and disease · 2024Article
- Soluble adenylyl cyclase contributes to imiquimod-mediated inflammation and is a potential therapeutic target in psoriasis.Experimental dermatology · 2023Article
- Using the Proteomics Toolbox to Resolve Topology and Dynamics of Compartmentalized cAMP Signaling.International journal of molecular sciences · 2023Review
- A non-catalytic N-terminus domain of WRN prevents mitotic telomere deprotection.Scientific reports · 2023Article
- Motif-Targeting Phosphoproteome Analysis of Cancer Cells for Profiling Kinase Inhibitors.Cancers · 2022Article
- Protein Kinase A Regulates Autophagy-Associated Proteins Impacting Growth and Virulence ofJournal of fungi (Basel, Switzerland) · 2022Article
- Interrogating Kinase-Substrate Relationships with Proximity Labeling and Phosphorylation Enrichment.Journal of proteome research · 2022Article
- Phosphoproteomic Analysis as an Approach for Understanding Molecular Mechanisms of cAMP-Dependent Actions.Molecular pharmacology · 2021Review
- Article
- dagLogo: An R/Bioconductor package for identifying and visualizing differential amino acid group usage in proteomics data.PloS one · 2020Article
- Phosphoproteomic identification of vasopressin V2 receptor-dependent signaling in the renal collecting duct.American journal of physiology. Renal physiology · 2019Article
- An ATR and CHK1 kinase signaling mechanism that limits origin firing during unperturbed DNA replication.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Targeting Adenosine in Cancer Immunotherapy to Enhance T-Cell Function.Frontiers in immunology · 2019Review
- Phosphatases control PKA-dependent functional microdomains at the outer mitochondrial membrane.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Design and Profiling of a Subcellular Targeted Optogenetic cAMP-Dependent Protein Kinase.Cell chemical biology · 2018Article
- Highly reproducible improved label-free quantitative analysis of cellular phosphoproteome by optimization of LC-MS/MS gradient and analytical column construction.Journal of proteomics · 2017Article
- Analyses of PDE-regulated phosphoproteomes reveal unique and specific cAMP-signaling modules in T cells.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In the past decade, mass-spectrometry-based methods have emerged for the quantitative profiling of dynamic changes in protein phosphorylation, allowing the behavior of thousands of phosphorylation sites to be monitored in a single experiment. However, when one is interested in specific signaling pathways, such shotgun methodologies are not ideal because they lack selectivity and are not cost and time efficient with respect to instrument and data analysis time. Here we evaluate and explore a peptide-centric antibody generated to selectively enrich peptides containing the cAMP-dependent protein kinase (PKA) consensus motif. This targeted phosphoproteomic strategy is used to profile temporal quantitative changes of potential PKA substrates in Jurkat T lymphocytes upon prostaglandin E2 (PGE2) stimulation, which increases intracellular cAMP, activating PKA. Our method combines ultra-high-specificity motif-based immunoaffinity purification with cost-efficient stable isotope dimethyl labeling. We identified 655 phosphopeptides, of which 642 (i.e. 98%) contained the consensus motif [R/K][R/K/X]X[pS/pT]. When our data were compared with a large-scale Jurkat T-lymphocyte phosphoproteomics dataset containing more than 10,500 phosphosites, a minimal overlap of 0.2% was observed. This stresses the need for such targeted analyses when the interest is in a particular kinase. Our data provide a resource of likely substrates of PKA, and potentially some substrates of closely related kinases. Network analysis revealed that about half of the observed substrates have been implicated in cAMP-induced signaling. Still, the other half of the here-identified substrates have been less well characterized, representing a valuable resource for future research.
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