Relationships between EGFR Signaling–competent and Endocytosis-competent Membrane Microdomains
Open Access
- 1 June 2005
- journal article
- Published by American Society for Cell Biology (ASCB) in Molecular Biology of the Cell
- Vol. 16 (6), 2704-2718
- https://doi.org/10.1091/mbc.e04-07-0596
Abstract
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.Keywords
This publication has 78 references indexed in Scilit:
- Caveolar and Lipid Raft Localization of the Growth Hormone Receptor and Its Signaling ElementsPublished by Elsevier ,2004
- Sliding doors: clathrin-coated pits or caveolae?Nature Cell Biology, 2003
- Fibroblast Growth Factor-2-induced Signaling through Lipid Raft-associated Fibroblast Growth Factor Receptor Substrate 2 (FRS2)Published by Elsevier ,2003
- Lipid rafts and B-cell activationNature Reviews Immunology, 2002
- Looking at lipid rafts?Trends in Cell Biology, 1999
- The Ear of α-Adaptin Interacts with the COOH-terminal Domain of the Eps15 ProteinPublished by Elsevier ,1996
- Clathrin assembly protein AP-2 induces aggregation of membrane vesicles: a possible role for AP-2 in endosome formation.The Journal of cell biology, 1992
- Caveolin, a protein component of caveolae membrane coatsCell, 1992
- Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical cell surfaceCell, 1992
- Lateral diffusion of epidermal growth factor complexed to its surface receptors does not account for the thermal sensitivity of patch formation and endocytosisBiochemistry, 1982