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Vol. 16, Issue 6, 2704-2718, June 2005
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* MicroScoBio Research Center, Department of Experimental Medicine, University of Genoa, 16132 Genoa, Italy;
Italian Foundation for Cancer Research (FIRC) Institute of Molecular Oncology (IFOM), 20139 Milan, Italy;
Department of Experimental Oncology, European Institute of Oncology, 20141 Milan, Italy; and
|| Department of Medicine, Surgery and Dentistry, University of Milan, 20142 Milan, Italy
Submitted July 16, 2004;
Revised March 7, 2005;
Accepted March 8, 2005
Monitoring Editor: Juan S. Bonifacino
Membrane microdomains, the so-called lipid rafts, function as platforms to concentrate receptors and assemble the signal transduction machinery. Internalization, in most cases, is carried out by different specialized structures, the clathrin-coated pits. Here, we show that several endocytic proteins are efficiently recruited to morphologically identified plasma membrane lipid rafts, upon activation of the epidermal growth factor (EGF) receptor (EGFR), a receptor tyrosine kinase. Analysis of detergent-resistant membrane fractions revealed that the EGF-dependent association of endocytic proteins with rafts is as efficient as that of signaling effector molecules, such as Grb2 or Shc. Finally, the EGFR, but not the nonsignaling transferrin receptor, could be localized in nascent coated pits that almost invariably contained raft membranes. Thus, specialized membrane microdomains have the ability to assemble both the molecular machineries necessary for intracellular propagation of EGFR effector signals and for receptor internalization.
Abbreviations used: RTK, receptor tyrosine kinases; EGFR, epidermal growth factor receptor; CCP, clathrin-coated pit; CCV, clathrin-coated vesicle; DRM, detergent-resistant membrane; GPI, glycosylphosphatidyl-inositol; HPR, horseradish peroxidase; CT-B/HRP, HRP-labeled cholera toxin B subunit; M
CD, methyl--cyclodextrin; PLAP, placental alkaline phosphatase; Tf, transferrin; TfR, transferrin receptor.
The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).
These authors contributed equally to this work.
Address correspondence to: Carlo Tacchetti (carlo.tacchetti{at}unige.it).
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