Am J Physiol Cell Physiol AJP: Gastrointestinal and Liver Physiology
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Am J Physiol Cell Physiol 275: C1419-C1428, 1998;
0363-6143/98 $5.00
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Vol. 275, Issue 6, C1419-C1428, December 1998

EDITORIAL FOCUS
Differential signaling and regulation of apical vs. basolateral EGFR in polarized epithelial cells

Scott K. Kuwada1,2,3, Kirk A. Lund4, Xiu Fen Li1, Peter Cliften4, Kurt Amsler5, Lee K. Opresko6, and H. Steven Wiley3,6

Divisions of 1 Gastroenterology and 4 Hematology/Oncology, Departments of Medicine and of 6 Pathology, University of Utah, 2 Department of Veterans Affairs Medical Center, and 3 Huntsman Cancer Institute, Salt Lake City, Utah 84132; and 5 Department of Physiology and Biophysics, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854

Overexpression of the epidermal growth factor receptors (EGFR) in polarized kidney epithelial cells caused them to appear in high numbers at both the basolateral and apical cell surfaces. We utilized these cells to look for differences in the regulation and signaling of apical vs. basolateral EGFR. Apical and basolateral EGFR were biologically active and mediated EGF-induced cell proliferation to similar degrees. Receptor downregulation and endocytosis were less efficient at the apical surface, resulting in prolonged EGF-induced tyrosine kinase activity at the apical cell membrane. Tyrosine phosphorylation of EGFR substrates known to mediate cell proliferation, Src-homologous and collagen protein (SHC), extracellularly regulated kinase 1 (ERK1), and ERK2 could be induced similarly by activation of apical or basolateral EGFR. Focal adhesion kinase was tyrosine phosphorylated more by basolateral than by apical EGFR; however, beta -catenin was tyrosine phosphorylated to a much greater degree following the activation of mislocalized apical EGFR. Thus EGFR regulation and EGFR-mediated phosphorylation of certain substrates differ at the apical and basolateral cell membrane domains. This suggests that EGFR mislocalization could result in abnormal signal transduction and aberrant cell behavior.

tyrosine phosphorylation; beta -catenin; proliferation; epidermal growth factor receptor downregulation and endocytosis


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