Regulation of the EphA2 Tyrosine Phosphorylation by the Human Cytoplasmic Protein Tyrosine Phosphatase
Abstract
Intracellular signaling by protein tyrosine phosphorylation is generally understood to govern many aspects of cellular behavior. The biological consequences of this signaling pathway are important because the levels of protein tyrosine phosphorylation are frequently elevated in cancer cells. In the classic paradigm, tyrosine kinases promote tumor cell growth, survival and invasiveness whereas tyrosine phosphatases negatively regulate these same behaviors. Here, we identify one particular tyrosine phosphatase, LMW-PTP, which is frequently overexpressed in transformed cells. We also show that overexpression of LMW-PTP is sufficient to confer malignant transformation upon non-transformed mammary epithelial cells. Notably, we show that the EphA2 receptor tyrosine kinase is a prominent substrate for LMW-PTP and that the oncogenic activities of LMW-PTP result from altered EphA2 expression and function. These results suggest a role for LMW-PTP in breast cancer progression and link its oncogenic potential to EphA2.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jun 01, 2002
- Accession Number
- ADB282209
Entities
People
- Elikplimi K. Asem
Organizations
- Purdue University