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Originally published as MBC in Press, 10.1091/mbc.E05-05-0456 on October 5, 2005

Vol. 16, Issue 12, 5832-5842, December 2005

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The Inhibitory Effect of ErbB2 on Epidermal Growth Factor-induced Formation of Clathrin-coated Pits Correlates with Retention of Epidermal Growth Factor Receptor-ErbB2 Oligomeric Complexes at the Plasma Membrane

Camilla Haslekås *, Kamilla Breen *, Ketil W. Pedersen, Lene E. Johannessen, Espen Stang, and Inger Helene Madshus

Institute of Pathology, University of Oslo, Rikshospitalet, 0027 Oslo, Norway

Submitted May 24, 2005; Revised September 13, 2005; Accepted September 23, 2005
Monitoring Editor: Jean Gruenberg

By constructing stably transfected cells harboring the same amount of epidermal growth factor (EGF) receptor (EGFR), but with increasing overexpression of ErbB2, we have demonstrated that ErbB2 efficiently inhibits internalization of ligand-bound EGFR. Apparently, ErbB2 inhibits internalization of EGF-bound EGFR by constitutively driving EGFR-ErbB2 hetero/oligomerization. We have demonstrated that ErbB2 does not inhibit phosphorylation or ubiquitination of the EGFR. Our data further indicate that the endocytosis deficiency of ErbB2 and of EGFR-ErbB2 heterodimers/oligomers cannot be explained by anchoring of ErbB2 to PDZ-containing proteins such as Erbin. Instead, we demonstrate that in contrast to EGFR homodimers, which are capable of inducing new clathrin-coated pits in serum-starved cells upon incubation with EGF, clathrin-coated pits are not induced upon activation of EGFR-ErbB2 heterodimers/oligomers.

This article was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E05-05-0456) on October 5, 2005.

Abbreviations used: PAE, porcine aortic endothelial.

* These authors contributed equally to this study.

Address correspondence to: Inger Helene Madshus (i.h.madshus{at}medisin.uio.no).




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