Journal:

Article Title: Grb2 Regulates Internalization of EGF Receptors through Clathrin-coated Pits

doi: 10.1091/mbc.E02-08-0532

Figure Lengend Snippet: Schematic representation of EGF receptor mutants. (A) Wild-type EGFR (WT) is drawn with the extracellular, transmembrane (TM) and intracellular domain (kinase and C terminus). Main tyrosine phosphorylation sites (residues 992, 1068, 1086, 1148, and 1173) and a Cbl binding site (Tyr1045) are indicated in WT receptor. Mutants have C-terminal truncation of 79 (C′1107), 96 (C′1090), 114 (C′1072), 123 (C′1063), and 164 amino acid residues (C′1022). Tyrosine substitutions by phenylalanines (F) are indicated. (B) To confirm the correct size of truncated EGFR mutants, PAE cells expressing WT, C′1107, C′1090, C′1072, C′1063, or C′1022 were lysed, and the EGFR was detected in lysates by immunoblotting with antibody 2913.

Article Snippet: Internalization of 125 I-EGF and 125 I-transferrin Mouse receptor-grade EGF was obtained from Collaborative Research Inc. (Bedford, MA) and iodinated using a modified chloramine T method as described previously ( Sorkin et al. , 1991 ).

Techniques: Binding Assay, Expressing, Western Blot