ArticleMolecular and cellular biology1991
Phosphorylation and activation of epidermal growth factor receptors in cells transformed by the src oncogene.
Article in Molecular and cellular biology, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 73 citations in OpenAlex.
- Light Sensing beyond Vision: Focusing on a Possible Role for the FICZ/AhR Complex in Skin Optotransduction.Cells · 2024Review
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- Cellular functions regulated by phosphorylation of EGFR on Tyr845.International journal of molecular sciences · 2013Review
- Tyrosine phosphorylation regulates maturation of receptor tyrosine kinases.Molecular and cellular biology · 2005Article
- Review
- Transformation of chicken embryo fibroblasts by v-src uncouples beta1 integrin-mediated outside-in but not inside-out signaling.Molecular and cellular biology · 2001Article
- Ligand-independent activation of platelet-derived growth factor receptor is a necessary intermediate in lysophosphatidic, acid-stimulated mitogenic activity in L cells.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- Tumor promotion by depleting cells of protein kinase C delta.Molecular and cellular biology · 1997Article
- Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents.The EMBO journal · 1996Article
- Mutation of a Src phosphorylation site in the PDGF beta-receptor leads to increased PDGF-stimulated chemotaxis but decreased mitogenesis.The EMBO journal · 1996Article
- Transformation of Rat-1 fibroblasts with the v-src oncogene induces inositol 1,4,5-trisphosphate 3-kinase expression.The Biochemical journal · 1996Article
- Transformation of Rat-1 fibroblasts with the v-src oncogene increases the tyrosine phosphorylation state and activity of the alpha subunit of Gq/G11.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Stimulation of growth factor receptor signal transduction by activation of voltage-sensitive calcium channels.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Potentiation of epidermal growth factor receptor-mediated oncogenesis by c-Src: implications for the etiology of multiple human cancers.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Identification of the in vitro phosphorylation sites on Gs alpha mediated by pp60c-src.The Biochemical journal · 1995Article
- Analysis of the role of the Shc and Grb2 proteins in signal transduction by the v-ErbB protein.Molecular and cellular biology · 1994Article
- Polyamines are essential for cell transformation by pp60v-src: delineation of molecular events relevant for the transformed phenotype.The Journal of cell biology · 1993Article
- The SH2/SH3 domain-containing protein Nck is recognized by certain anti-phospholipase C-gamma 1 monoclonal antibodies, and its phosphorylation on tyrosine is stimulated by platelet-derived growth factor and epidermal growth factor treatment.Molecular and cellular biology · 1992Article
- Effects of SH2 and SH3 deletions on the functional activities of wild-type and transforming variants of c-Src.Molecular and cellular biology · 1992Article
- Identification and characterization of a novel cytoskeleton-associated pp60src substrate.Molecular and cellular biology · 1991Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Because functionally significant substrates for the tyrosyl protein kinase activity of pp60v-src are likely to include membrane-associated proteins involved in normal growth control, we have tested the hypothesis that pp60v-src could phosphorylate and alter the signaling activity of transmembrane growth factor receptors. We have found that the epidermal growth factor (EGF) receptor becomes constitutively phosphorylated on tyrosine in cells transformed by the src oncogene and in addition displays elevated levels of phosphoserine and phosphothreonine. High-performance liquid chromatography phosphopeptide mapping revealed two predominant sites of tyrosine phosphorylation, both of which differed from the major sites of receptor autophosphorylation; thus, the src-induced phosphorylation is unlikely to occur via an autocrine mechanism. To determine whether pp60v-src altered the signaling activity of the EGF receptor, we analyzed the tyrosine phosphorylation of phospholipase C-gamma, since phosphorylation of this enzyme occurs in response to activation of the EGF receptor but not in response to pp60v-src alone. We found that in cells coexpressing pp60v-src and the EGF receptor, phospholipase C-gamma was constitutively phosphorylated, a result we interpret as indicating that the signaling activity of the EGF receptor was altered in the src-transformed cells. These findings suggest that pp60v-src-induced alterations in phosphorylation and function of growth regulatory receptors could play an important role in generating the phenotypic changes associated with malignant transformation.
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