Functional Interactions Between c-Src and HER1 Potentiate Neoplastic Transformation: Implications for the Etiology of Human Breast Cancer
Abstract
In cells where the EGF receptor and pp60c-Src are overexpressed, such as a fibroblast model system or in certain human breast cancer cell lines, these two tyrosine kinases interact physically and functionally to promote tumorigenesis. When in association with c-Src, the EGFR becomes phosphorylated within the kinase domain on Tyr 845. Kinase activity of c-Src is required for this phosphorylation to occur, indicating that Tyr 845 is likely a direct target for the c-Src kinase. Tyr 845 phosphorylation occurs in response to a variety of 0-protein coupled and cytokine receptor coupled signaling pathways; and c-Src kinase activity is required for this phosphorylation to occur.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 01, 2000
- Accession Number
- ADB263453
Entities
People
- Jacqueline Biscardi
- Parsons
Organizations
- University of Virginia