ArticleCancer biology & therapy2011
Src family kinases mediate epidermal growth factor receptor signaling from lipid rafts in breast cancer cells.
Article in Cancer biology & therapy, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 81 citations in OpenAlex.
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- Suppressing Src-Mediated EGFR Signaling by Sustained Calcium Supply Targeting Triple-Negative Breast Cancer.International journal of molecular sciences · 2023Article
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- Cholesterol promotes EGFR-TKIs resistance in NSCLC by inducing EGFR/Src/Erk/SP1 signaling-mediated ERRα re-expression.Molecular cancer · 2022Article
- Development of a novel spatiotemporal depletion system for cellular cholesterol.Journal of lipid research · 2022Article
- 3, 3'- (3, 5-DCPBC) Down-Regulates Multiple Phosphokinase Dependent Signal Transduction Pathways in Malignant Melanoma Cells through Specific Diminution of EGFRMolecules (Basel, Switzerland) · 2022Article
- Our evolving understanding of how 27-hydroxycholesterol influences cancer.Biochemical pharmacology · 2022Review
- The inhibition of Panc1 cancer cells invasion by hAMSCs secretome through suppression of tyrosine phosphorylation of SGK223 (at Y411 site), c-Src (at Y416, Y530 sites), AKT activity, and JAK1/Stat3 signaling.Medical oncology (Northwood, London, England) · 2022Article
- Lipids in Pathophysiology and Development of the Membrane Lipid Therapy: New Bioactive Lipids.Membranes · 2021Review
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Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Activation of the epidermal growth factor receptor (EGFR) regulates cellular proliferation, survival, and migration of breast cancer cells. In particular, EGFR recruits signaling proteins to the cell membrane leading to their phosphorylation and activation. However, EGFR also localizes to other cellular structures, including endosomes, mitochondrion, and nuclei. Recently, we demonstrated that lipid raft localization of EGFR in triple-negative breast cancer cell lines promotes EGFR protein-dependent, EGFR kinase-independent activation of Akt. Here, we further define the mechanism by which lipid rafts regulate EGFR signaling to Akt. Specifically, we show that the non-receptor tyrosine kinase c-Src co-localizes and co-associates with EGFR and lipid rafts. Breast cancer cells resistant to treatment with EGFR inhibitors, were also resistant to treatment with Src family kinase (SFK) inhibitors; however, the combination of EGFR and SFK inhibitors synergistically decreases cell viability. We found that this decrease in cell viability observed with EGFR and SFK inhibitor co-treatment correlates with loss of Akt phosphorylation. In addition, we found that in breast cancer cell lines with EGFR and c-Src co-localized to lipid rafts, phospho-inositide 3 kinase (PI3K) was also associated with lipid rafts. Together, the data herein suggest that lipid rafts provide a platform for the interaction of EGFR, c-Src, and PI3K, leading to activation of cellular survival signaling in breast cancer cells.
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