Dimerization and higher-order oligomerization are believed to play an important role in the activation of the EGFR (epidermal growth factor receptor). Understanding of the process has been limited by the lack of availability of suitable methods for the measurement in cells of distances in the range 10–100 nm, too short for imaging methods and too long for spectroscopic methods such as FRET. In the present article, we review the current state of our knowledge of EGFR oligomerization, and describe results from a new single-molecule localization method that has allowed the quantitative characterization of the distribution of EGFR–EGFR distances in cells. Recent data suggest the involvement of cortical actin in regulating the formation of EGFR complexes.
Structure–function relationships and supramolecular organization of the EGFR (epidermal growth factor receptor) on the cell surface
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Sarah R. Needham, Laura C. Zanetti-Domingues, Michael Hirsch, Daniel J. Rolfe, Christopher J. Tynan, Selene K. Roberts, Marisa L. Martin-Fernandez, David T. Clarke; Structure–function relationships and supramolecular organization of the EGFR (epidermal growth factor receptor) on the cell surface. Biochem Soc Trans 1 February 2014; 42 (1): 114–119. doi: https://doi.org/10.1042/BST20130236
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