ArticleThe Journal of biological chemistry2009
Tyrosine phosphorylation of the human glutathione S-transferase P1 by epidermal growth factor receptor.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 47 citations in OpenAlex.
- Beyond the Very Important Pharmacogenes (VIPs): Uncovering Shadow Pharmacogenes in the Human Drug Response Network.ACS omega · 2026Article
- Parallel phosphoproteomics and metabolomics map the global metabolic tyrosine phosphoproteome.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Multiscale photocatalytic proximity labeling reveals cell surface neighbors on and between cells.Science (New York, N.Y.) · 2024Article
- Article
- The Multifaceted Role of Glutathione S-Transferases in Health and Disease.Biomolecules · 2023Review
- NBDHEX re-sensitizes adriamycin-resistant breast cancer by inhibiting glutathione S-transferase pi.Cancer medicine · 2023Article
- Development and biological applications of sulfur-triazole exchange (SuTEx) chemistry.RSC chemical biology · 2021Article
- Liganding Functional Tyrosine Sites on Proteins Using Sulfur-Triazole Exchange Chemistry.Journal of the American Chemical Society · 2020Article
- GlutathioneFrontiers in immunology · 2018Article
- Phosphorylation of Glutathione S-Transferase P1 (GSTP1) by Epidermal Growth Factor Receptor (EGFR) Promotes Formation of the GSTP1-c-Jun N-terminal kinase (JNK) Complex and Suppresses JNK Downstream Signaling and Apoptosis in Brain Tumor Cells.The Journal of biological chemistry · 2015Article
- Transcriptional responses of glutathione transferase genes in Ruditapes philippinarum exposed to microcystin-LR.International journal of molecular sciences · 2015Article
- Survey of phosphorylation near drug binding sites in the Protein Data Bank (PDB) and their effects.Proteins · 2015Article
- Mitogen-activated protein kinase (MAPK) hyperactivation and enhanced NRAS expression drive acquired vemurafenib resistance in V600E BRAF melanoma cells.The Journal of biological chemistry · 2014Article
- Glutathione S-transferase Pi expression predicts response to adjuvant chemotherapy for stage C colon cancer: a matched historical control study.BMC cancer · 2012Article
- Activation of multiple ERBB family receptors mediates glioblastoma cancer stem-like cell resistance to EGFR-targeted inhibition.Neoplasia (New York, N.Y.) · 2012Article
- Growth-inhibitory and chemosensitizing effects of the glutathione-S-transferase-π-activated nitric oxide donor PABA/NO in malignant gliomas.International journal of cancer · 2012Article
- Analysis of EGFR signaling pathway in nasopharyngeal carcinoma cells by quantitative phosphoproteomics.Proteome science · 2011Article
- Regulatory functions of glutathione S-transferase P1-1 unrelated to detoxification.Drug metabolism reviews · 2011Review
- Regulation of benzo[a]pyrene-mediated DNA- and glutathione-adduct formation by 2,3,7,8-tetrachlorodibenzo-p-dioxin in human lung cells.Chemical research in toxicology · 2011Article
- Regional treatment strategies for in-transit melanoma metastasis.Surgical oncology clinics of North America · 2011Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Epidermal growth factor receptor (EGFR) gene amplification, mutations, and/or aberrant activation are frequent abnormalities in malignant gliomas and other human cancers and have been associated with an aggressive clinical course and a poor therapeutic outcome. Elevated glutathione S-transferase P1 (GSTP1), a major drug-metabolizing and stress response signaling protein, is also associated with drug resistance and poor clinical outcome in gliomas and other cancers. Here, we provide evidence that GSTP1 is a downstream EGFR target and that EGFR binds to and phosphorylates tyrosine residues in the GSTP1 protein in vitro and in vivo. Mass spectrometry and mutagenesis analyses in a cell-free system and in gliomas cells identified Tyr-7 and Tyr-198 as major EGFR-specific phospho-acceptor residues in the GSTP1 protein. The phosphorylation increased GSTP1 enzymatic activity significantly, and computer-based modeling showed a corresponding increase in electronegativity of the GSTP1 active site. In human glioma and breast cancer cells, epidermal growth factor stimulation rapidly increased GSTP1 tyrosine phosphorylation and decreased cisplatin sensitivity. Lapatinib, a clinically active EGFR inhibitor, significantly reversed the epidermal growth factor-induced cisplatin resistance. These data define phosphorylation and activation of GSTP1 by EGFR as a novel, heretofore unrecognized component of the EGFR signaling network and a novel mechanism of tumor drug resistance, particularly in tumors with elevated GSTP1 and/or activated EGFR.
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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.