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First published online 24 July 2007
doi: 10.1242/jcs.007658

Journal of Cell Science 120, 2763-2773 (2007)
Published by The Company of Biologists 2007
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Research Article

Mapping ErbB receptors on breast cancer cell membranes during signal transduction

Shujie Yang1,*, Mary Ann Raymond-Stintz1,*, Wenxia Ying2, Jun Zhang3, Diane S. Lidke1, Stanly L. Steinberg2, Lance Williams3, Janet M. Oliver1 and Bridget S. Wilson1,{ddagger}

1 Department of Pathology and Cancer Research and Treatment Center, University of New Mexico, Albuquerque, NM 87131, USA
2 Department of Mathematics and Statistics, University of New Mexico, Albuquerque, NM 87131, USA
3 Department of Computer Science, University of New Mexico, Albuquerque, NM 87131, USA

{ddagger} Author for correspondence (e-mail: bwilson{at}salud.unm.edu)

Accepted 12 June 2007

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.

Key words: ErbB, Microdomains, Shc, PI 3-kinase, STAT5


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© The Company of Biologists Ltd 2007