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JCS ePress online publication date 24 Jul 2007
doi: 10.1242/jcs.007658


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Research Article

Mapping ErbB receptors on breast cancer cell membranes during signal transduction


Shujie Yang, Mary Ann Raymond-Stintz, Wenxia Ying, Jun Zhang, Diane S. Lidke, Stanly L. Steinberg, Lance Williams, Janet M. Oliver, and Bridget S. Wilson*
* Author for correspondence (e-mail: bwilson{at}salud.unm.edu)

Distributions of ErbB receptors on membranes of SKBR3 breast cancer cells were mapped by immunoelectron microscopy. The most abundant receptor, ErbB2, is phosphorylated, clustered and active. Kinase inhibitors ablate ErbB2 phosphorylation without dispersing clusters. Modest co-clustering of ErbB2 and EGFR, even after EGF treatment, suggests that both are predominantly involved in homointeractions. Heregulin leads to dramatic clusters of ErbB3 that contain some ErbB2 and EGFR and abundant PI 3-kinase. Other docking proteins, such as Shc and STAT5, respond differently to receptor activation. Levels of Shc at the membrane increase two- to five-fold with EGF, whereas pre-associated STAT5 becomes strongly phosphorylated. These data suggest that the distinct topography of receptors and their docking partners modulates signaling activities.




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A. Szabo, G. Horvath, J. Szollosi, and P. Nagy
Quantitative Characterization of the Large-Scale Association of ErbB1 and ErbB2 by Flow Cytometric Homo-FRET Measurements
Biophys. J., August 15, 2008; 95(4): 2086 - 2096.
[Abstract] [Full Text] [PDF]




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