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EGF receptor family: twisting targets for improved cancer therapies
Authors:Antony W. Burgess  Yoav I. Henis  Nancy E. Hynes  Thomas Jovin  Alexander Levitzki  Ronit Pinkas-Kramarski
Affiliation:1. The Walter &2. Eliza Hall Institute of Medical Research, Burgess Lab Structural BiologyParkvilleAustraliatburgess@wehi.edu.au;4. Department of Neurobiology, George S. Wise Faculty of Life Sciences, Tel Aviv UniversityTel AvivIsrael;5. Department of Mechanisms of Cancer, Friedrich Miescher Institute for Biomedical ResearchMaulbeerstrasse, BaselSwitzerland;6. Laboratory of Cellular Dynamics, Max Planck Institute for Biophysical ChemistryG?ttingenGermany;7. Department of Biological Chemistry, Unit of Cellular Signaling, Alexander Siberman Institute of Life Sciences, Hebrew University of JerusalemJerusalemIsrael
Abstract:Abstract

The epidermal growth factor receptor (EGFR) undergoes a conformational change in response to ligand binding. The ligand-induced changes in cell surface aggregation and mobility have a profound effect on the function of all the family members. Ligand also activates the EGFR intracellular kinase, stimulating proliferation and cell survival. The EGFR family are often activated, overexpressed or mutated in cancer cells and therapeutic drugs (including antibodies) can slow the progress of some cancers. This article provides a brief, annotated summary of the presentations and discussion which occurred at the Epidermal Growth Factor Receptor – Future Directions Conference held in Jerusalem in November 2013.
Keywords:Cell surface  erbB2  erbB3  FLIM  FRET  receptor dynamics  therapeutic antibodies
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