Abstract
The intracellular juxtamembrane domain of several receptor tyrosine kinases (RTKs) has been proposed to play an autoinhibitory role. The epidermal growth factor receptor (EGFR) has been widely used as a model in studies of the RTK activation mechanism. Extensive efforts have been devoted to studying the functions of EGFR's different domains; however, the role of the juxtamembrane domain in EGFR phosphorylation and activation is yet to be clarified. In this work, we replaced the 30 amino acids (674-704) of the EGF juxtamembrane domain with ten repeats of Glycine-Glycine-Serine (GGS). Preliminary results from western blots showed decreased phosphorylation of Tyr1148 in the EGFR-GGS chimeric receptor, which suggests that the juxtamembrane domain of EGFR plays an activating role rather than an inhibitory one. Currently we are using ligand titration and Foster resonance energy transfer (FRET) experiments to further explore the difference between wild type EGFR and the EGFR-GGS chimeric receptor. Results from this work will yield further insights into the function of the juxtamembrane domain in the EGFR activation process.
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