Trans-regulation of epidermal growth factor receptor by lysophosphatidic acid and G protein-coupled receptors
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Updated: Sep 30, 2026

Studying the Stoichiometry of Epidermal Growth Factor Receptor in Intact Cells using Correlative Microscopy
Published on: September 11, 2015
1Molecular Oncology Program, H. Lee Moffitt Cancer Center and Research Institute, Tampa, FL 33612, USA. wu@moffitt.usf.edu
Abstract:
Lysophosphatidic acid (LPA) is known to induce protein tyrosine phosphorylation and has growth factor-like effects. In the last several years, the epidermal growth factor (EGF) receptor has been recognized as a protein tyrosine kinase that plays a central role in mediating LPA-induced tyrosine phosphorylation and Erk MAP kinase activation. In this article, we review recent progress in the study of trans-regulation of EGF receptor by LPA and G protein-coupled receptors (GPCR) and discuss the gap in our knowledge of the mechanism by which LPA induces EGF receptor activation.
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