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

Journal: The Journal of Biological Chemistry

Article Title: Quantitation of the Effect of ErbB2 on Epidermal Growth Factor Receptor Binding and Dimerization *

doi: 10.1074/jbc.M112.373647

Figure Lengend Snippet: Binding of 125I-EGF to cells expressing EGF receptors and ErbB2. A, 125I-EGF binding to cells expressing ∼300,000 EGF receptors and the indicated number of ErbB2 molecules. The level of ErbB2 was measured by the binding of 125I-trastuzumab. B, model for the binding of EGF to EGFR homodimers and EGFR/ErbB2 heterodimers. Open circles represent EGF receptor molecules. Hatched circles represent ErbB2 molecules. E is a bound EGF molecule. The term that refers to the equilibrium association constant for each interaction is indicated over the arrows. Fitted values for the equilibrium association constants are shown. Values in red indicate the values that were fitted to Equation 1 based on the binding data in panel A. Values in black were set as constants during the fitting and are based on previous studies of EGF binding to only the EGF receptor. Values in gray were calculated based on the principle of microscopic equilibrium.

Article Snippet: 125 I-EGF and 125 I-Trastuzumab Synthesis and Binding Analyses Murine EGF (Biomedical Technologies, Inc.) and trastuzumab (Barnes Hospital pharmacy) were radiolabeled with 125 I using the ICl method ( 24 ).

Techniques: Binding Assay, Expressing