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Papers In Press, published online ahead of print December 10, 2001
J. Biol. Chem, 10.1074/jbc.M108681200
Submitted on September 7, 2001
Revised on December 5, 2001
Accepted on December 10, 2001

The single transmembrane domains of erbB receptors self-associate in cell membranes

Jeannine M. Mendrola, Mitchell B. Berger, Megan C. King, and Mark A. Lemmon

Dept. of Biochemistry & Biophysics, University of Pennsylvania School of Medicine, Philadelphia, PA 19104-6059

Corresponding Author: mlemmon{at}mail.med.upenn.edu

Members of the epidermal growth factor (EGF) receptor, or erbB, family of receptor tyrosine kinases (RTK’s) have a single transmembrane (TM) alpha-helix that is usually assumed to play a passive role in ligand-induced dimerization and activation of the receptor. However, recent studies with the EGF receptor (erbB1) and the erythropoietin receptor have indicated that interactions between TM a-helices do contribute to stabilization of ligand-independent and/or ligand-induced receptor dimers. In addition, not all of the expected erbB receptor ligand-induced dimerization events can be recapitulated using isolated extracellular domains, suggesting that other regions of the receptor, such as the TM domain, may contribute to dimerization in vivo. Using an approach for analyzing TM domain interactions in E. coli cell membranes, named TOXCAT, we find that the TM domains of erbB receptors self-associate strongly in the absence of their extracellular domains, with the rank order erbB4-TM > erbB1-TM = erbB2-TM > erbB3-TM. A limited mutational analysis suggests that dimerization of these TM domains involves one or more GxxxG motifs, which occur frequently in the TM domains of RTK’s and are critical for stabilizing the glycophorin A (GpA) TM domain dimer. We also analyzed the effect of the valine to glutamic acid mutation in erbB2 that constitutively activates this receptor. Contrary to our expectations, this mutation reduced rather than increased erbB2-TM dimerization. Our findings suggest a role for TM domain interactions in erbB receptor function, possibly in stabilizing inactive ligand-independent receptor dimers that have been observed by several groups.


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