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J Biol Chem, Vol. 273, Issue 27, 16639-16642, July 3, 1998

COMMUNICATION
High-affinity Binding of Epidermal Growth Factor (EGF) to EGF Receptor Is Disrupted by Overexpression of Mutant Dynamin (K44A)

Tove Ringerike, Espen Stang, Lene E. Johannessen, Dagny Sandnes^§, Finn Olav Levy^¶, and Inger Helene Madshus

From the  Institute of Pathology, ^¶ MSD Cardiovascular Research Center, and  Institute for Surgical Research, University of Oslo, The National Hospital, N-0027 Oslo and the ^§ Department of Pharmacology, University of Oslo, P. O. Box 1057, N-0316 Oslo, Norway

Activation of the epidermal growth factor receptor (EGFR) kinase was analyzed in cells conditionally defective for clathrin-dependent endocytosis by overexpression of mutant dynamin (K44A). EGF-induced autophosphorylation of the EGFR on ice was strongly reduced in cells overexpressing mutant dynamin, and consistently, binding analyses showed that high-affinity EGFRs were lost. In the absence of mutant dynamin the cells displayed both high- and low-affinity EGFR. At 4 °C EGF-EGFR localized mainly outside coated pits regardless of expression of mutant dynamin. However, also low-affinity EGFR efficiently moved to coated pits upon incubating cells at 37 °C. Thus, expression of mutant dynamin disrupts high-affinity binding of EGF, but not ligand-induced recruitment of EGFR to clathrin-coated pits.

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Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.

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