Epidermal growth factor receptor signaling

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Epidermal growth factor receptor signaling Sven Bogdan, Christian Klämbt Current Biology Volume 11, Issue 8, Pages R292-R295 (April 2001) DOI: 10.1016/S0960-9822(01)00167-1

Fig. 1 EGFR structure. The EGFR is a monomer consisting of 1186 amino acids. Its extracellular domain is characterized by two cysteine-rich motifs (CR I and CRII). DER and Let-23 have an additional CRIII domain. The overall amino acid identity between the human ErbB1 and Let-23 proteins is 29% and that between DER and ErbB1 is 38%. Amino acids in EGFR that can be phosphorylated are indicated. TM, transmembrane domain; JM, juxtamembrane region. Current Biology 2001 11, R292-R295DOI: (10.1016/S0960-9822(01)00167-1)

Fig. 2 Downstream of EGFR. EGFR activity is transduced to the cell via a number of conserved signaling cascades. For details see text. Phosphorylated tyrosine residues of the EGFR recruit various adapter proteins with SH2 or PTB domains to the membrane: Y992, docking site of PLCγ; Y1045, docking site of Cbl; Y1068 and Y1086, docking sites of Grb2—Drk in Drosophila, Sem5 in C. elegans; Y1148 and Y1173, docking sites of Shc, Shp1 and PLCγ. Current Biology 2001 11, R292-R295DOI: (10.1016/S0960-9822(01)00167-1)

Fig. 3 Negative regulators of EGFR signaling. Several proteins were found to attenuate EGFR signaling. Argos, Decorin, and Kekkon bind to the extracellular domain of the EGFR. PKC is able to phosphorylate the EGFR at T654. Binding of Cbl at Y1045 results in ubiquitination and subsequent degradation. The recently identified Echinoid protein interferes with EGFR signaling downstream. LRR, leucine-rich repeat; Ig, immunoglobulin-like domain; FnIII, fibronectin type III repeat. Current Biology 2001 11, R292-R295DOI: (10.1016/S0960-9822(01)00167-1)