Publication Date:
2019
Description:
〈p〉Publication date: Available online 8 July 2019〈/p〉
〈p〉〈b〉Source:〈/b〉 Biochimica et Biophysica Acta (BBA) - Biomembranes〈/p〉
〈p〉Author(s): Deo R. Singh, Christopher King, Matt Salotto, Kalina Hristova〈/p〉
〈div xml:lang="en"〉
〈h5〉Abstract〈/h5〉
〈div〉〈p〉EGFR is a receptor tyrosine kinase that plays a critical role in cell proliferation, differentiation, survival and migration. Its activating ligand, EGF, has long been believed to stabilize the EGFR dimer. Two research studies aimed at quantitative measurements of EGFR dimerization, however, have led to contradicting conclusions and have questioned this view. Given the controversy, here we sought to measure the dimerization of EGFR in the absence and in the presence of saturating EGF concentrations, and to tease out the effect of ligand on dimer stability, using a FRET-based quantitative method. Our measurements show that the dissociation constant is decreased ~150 times due to ligand binding, indicative of significant dimer stabilization. In addition, our measurements demonstrate that EGF binding induces a conformational change in the EGFR dimer.〈/p〉〈/div〉
〈/div〉
〈div xml:lang="en"〉
〈h5〉Graphical abstract〈/h5〉
〈div〉〈p〉〈figure〉〈img src="https://ars.els-cdn.com/content/image/1-s2.0-S0005273619301476-ga1.jpg" width="265" alt="Unlabelled Image" title="Unlabelled Image"〉〈/figure〉〈/p〉〈/div〉
〈/div〉
Print ISSN:
0005-2736
Electronic ISSN:
1879-2642
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
,
Physics
