ArticleProceedings of the National Academy of Sciences of the United States of America2000
Analysis of receptor signaling pathways by mass spectrometry: identification of vav-2 as a substrate of the epidermal and platelet-derived growth factor receptors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed, 407 citations in OpenAlex.
- Decoding Rho GTPase signalling networks in directed cell migration.Frontiers in cell and developmental biology · 2026Review
- Cracking Lysine Crotonylation (Kcr): Enlightening a Promising Post-Translational Modification.Chembiochem : a European journal of chemical biology · 2025Review
- The Roles of RAC1 and RAC1B in Colorectal Cancer and Their Potential Contribution to Cetuximab Resistance.Cancers · 2024Review
- Proteomic Alteration in the Progression of Multiple Myeloma: A Comprehensive Review.Diagnostics (Basel, Switzerland) · 2023Review
- Pilot investigation of magnetic nanoparticle-based immobilized metal affinity chromatography for efficient enrichment of phosphoproteoforms for mass spectrometry-based top-down proteomics.Analytical and bioanalytical chemistry · 2023Article
- Platelets-related signature based diagnostic model in rheumatoid arthritis using WGCNA and machine learning.Frontiers in immunology · 2023Article
- Vav2 is a novel APP-interacting protein that regulates APP protein level.Scientific reports · 2022Article
- Vav Proteins in Development of the Brain: A Potential Relationship to the Pathogenesis of Congenital Zika Syndrome?Viruses · 2022Review
- Binding Affinity Determines Substrate Specificity and Enables Discovery of Substrates for N-Myristoyltransferases.ACS catalysis · 2021Article
- Proteomic Interrogation in Cancer Biomarker.Advances in experimental medicine and biology · 2021Article
- VAV2 signaling promotes regenerative proliferation in both cutaneous and head and neck squamous cell carcinoma.Nature communications · 2020Article
- The guanine nucleotide exchange factor VAV3 participates in ERBB4-mediated cancer cell migration.The Journal of biological chemistry · 2020Article
- Advances in development of new tools for the study of phosphohistidine.Laboratory investigation; a journal of technical methods and pathology · 2018Review
- A Conserved GEF for Rho-Family GTPases Acts in an EGF Signaling Pathway to Promote Sleep-like Quiescence in Caenorhabditis elegans.Genetics · 2016Article
- Ablation of Dicer leads to widespread perturbation of signaling pathways.Biochemical and biophysical research communications · 2015Article
- Low-bias phosphopeptide enrichment from scarce samples using plastic antibodies.Scientific reports · 2015Article
- Sensitive measurement of total protein phosphorylation level in complex protein samples.The Analyst · 2015Article
- Refined phosphopeptide enrichment by phosphate additive and the analysis of human brain phosphoproteome.Proteomics · 2015Article
- Protein expression patterns in two Spiraea species in response to cold treatment.Molecular biology reports · 2014Article
- Threonine 680 phosphorylation of FLJ00018/PLEKHG2, a Rho family-specific guanine nucleotide exchange factor, by epidermal growth factor receptor signaling regulates cell morphology of Neuro-2a cells.The Journal of biological chemistry · 2014Article
24 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Oligomerization of receptor protein tyrosine kinases such as the epidermal growth factor receptor (EGFR) by their cognate ligands leads to activation of the receptor. Transphosphorylation of the receptor subunits is followed by the recruitment of signaling molecules containing src homology 2 (SH2) or phosphotyrosine interaction domains (PID). Additionally, several cytoplasmic proteins that may or may not associate with the receptor undergo tyrosine phosphorylation. To identify several components of the EGFR signaling pathway in a single step, we have immunoprecipitated molecules that are tyrosine phosphorylated in response to EGF and analyzed them by one-dimensional gel electrophoresis followed by mass spectrometry. Combining matrix-assisted laser desorption/ionization (MALDI) and nanoelectrospray tandem mass spectrometry (MS/MS) led to the identification of nine signaling molecules, seven of which had previously been implicated in EGFR signaling. Several of these molecules were identified from low femtomole levels of protein loaded onto the gel. We identified Vav-2, a recently discovered guanosine nucleotide exchange factor that is expressed ubiquitously, as a substrate of the EGFR. We demonstrate that Vav-2 is phosphorylated on tyrosine residues in response to EGF and associates with the EGFR in vivo. Binding of Vav-2 to the EGFR is mediated by the SH2 domain of Vav-2. In keeping with its ubiquitous expression, Vav-2 seems to be a general signaling molecule, since it also associates with the platelet-derived growth factor (PDGF) receptor and undergoes tyrosine phosphorylation in fibroblasts upon PDGF stimulation. The strategy suggested here can be used for routine identification of downstream components of cell surface receptors in mammalian cells.
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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.