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Biophys. J. BioFAST: First Published May 11, 2007. doi:10.1529/biophysj.107.105494
© 2007 by the Biophysical Society.

A more recent version of this article appeared on August 1, 2007.
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SPECTROSCOPY, IMAGING, OTHER TECHNIQUES

Oligomerization of the EGF Receptor Investigated by Live Cell Fluorescence Intensity Distribution Analysis

Saveez Saffarian 1, Yu Li 2, Elliot L Elson 1 and Linda J Pike 1*

1 Washington University School of Medicine
2 Washington University

* To whom correspondence should be addressed. E-mail: pike{at}biochem.wustl.edu.

Submitted on January 29, 2007
Revised on March 5, 2007
Accepted on 27 March 2007


  Abstract
Recent evidence suggests that the EGF receptor oligomerizes or clusters in cells even in the absence of agonist ligand. To assess the status of EGF receptors in live cells, an EGF receptor fused to eGFP was stably expressed in CHO cells and studied using fluorescence correlation spectroscopy and fluorescent brightness analysis. By modifying FIDA for use in a two-dimensional system with quantal brightnesses, a method was developed to quantify the degree of clustering of the receptors on the cell surface. The analysis demonstrates that under physiological conditions, the EGF receptor exists in a complex equilibrium involving single molecules and clusters of two or more receptors. Acute depletion of cellular cholesterol enhanced EGF receptor clustering while cholesterol loading decreased receptor clustering, indicating that receptor aggregation is sensitive to the lipid composition of the membrane.

Key Words: Cholesterol, EGF receptor, Fluorescence correlation spectroscopy, Fluorescence intensity distribution analysis




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Copyright © 2007 by the Biophysical Society.