ArticleAnalytical chemistry2014
Global phosphoproteomics of activated B cells using complementary metal ion functionalized soluble nanopolymers.
Article in Analytical chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- Current Methods of Post-Translational Modification Analysis and Their Applications in Blood Cancers.Cancers · 2021Review
- Titanium(IV)-functionalized zirconium-organic frameworks as dual-metal affinity probe for recognition of endogenous phosphopeptides prior to mass spectrometric quantification.Mikrochimica acta · 2019Article
- Identification of Phosphorylated Proteins on a Global Scale.Current protocols in chemical biology · 2018Article
- Altering the Peptide Binding Selectivity of Polymeric Reverse Micelle Assemblies via Metal Ion Loading.Langmuir : the ACS journal of surfaces and colloids · 2017Article
- Understanding Epstein-Barr Virus Life Cycle with Proteomics: A Temporal Analysis of Ubiquitination During Virus Reactivation.Omics : a journal of integrative biology · 2017Article
- Quantitative Phosphoproteomic Analysis of T-Cell Receptor Signaling.Methods in molecular biology (Clifton, N.J.) · 2017Article
- Quantitative proteomics and terminomics to elucidate the role of ubiquitination and proteolysis in adaptive immunity.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2016Review
- Multiplexed Imaging of Protein Phosphorylation on Membranes Based on Ti(IV) Functionalized Nanopolymers.Chembiochem : a European journal of chemical biology · 2016Article
- Comparing multistep immobilized metal affinity chromatography and multistep TiO2 methods for phosphopeptide enrichment.Analytical chemistry · 2015Article
- Protein networks and activation of lymphocytes.Current opinion in immunology · 2015Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Engagement of the B cell receptor for antigen (BCR) leads to immune responses through a cascade of intracellular signaling events. Most studies to date have focused on the BCR and protein tyrosine phosphorylation. Because spleen tyrosine kinase, Syk, is an upstream kinase in multiple BCR-regulated signaling pathways, it also affects many downstream events that are modulated through the phosphorylation of proteins on serine and threonine residues. Here, we report a novel phosphopeptide enrichment strategy and its application to a comprehensive quantitative phosphoproteomics analysis of Syk-dependent downstream signaling events in B cells, focusing on serine and threonine phosphorylation. Using a combination of the Syk inhibitor piceatannol, SILAC quantification, peptide fractionation, and complementary PolyMAC-Ti and PolyMAC-Zr enrichment techniques, we analyzed changes in BCR-stimulated protein phosphorylation that were dependent on the activity of Syk. We identified and quantified over 13,000 unique phosphopeptides, with a large percentage dependent on Syk activity in BCR-stimulated B cells. Our results not only confirmed many known functions of Syk, but more importantly, suggested many novel roles, including in the ubiquitin proteasome pathway, that warrant further exploration.
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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.