High-affinity binding of epidermal growth factor (EGF) to EGF receptor is disrupted by overexpression of mutant dynamin (K44A).

The Journal of Biological Chemistry
T RingerikeI H Madshus

Abstract

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 degreesC 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 degreesC. 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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Citations

Aug 5, 2000·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·G Carpenter
Apr 30, 2002·Trends in Cell Biology·Boris N Kholodenko
Aug 16, 2002·European Journal of Biochemistry·Kristi G BacheHarald Stenmark
Mar 1, 2012·Proceedings of the National Academy of Sciences of the United States of America·Leiliane P SousaJoseph Schlessinger
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