Effect of phosphorylation on EGFR dimer stability probed by single-molecule dynamics and FRET/FLIM.

ABSTRACT: Deregulation of epidermal growth factor receptor (EGFR) signaling has been correlated with the development of a variety of human carcinomas. EGF-induced receptor dimerization and consequent trans- auto-phosphorylation are among the earliest events in signal transduction. Binding of EGF is thought to induce a conformational change that consequently unfolds an ectodomain loop required for dimerization indirectly. It may also induce important allosteric changes in the cytoplasmic domain. Despite extensive knowledge on the physiological activation of EGFR, the effect of targeted therapies on receptor conformation is not known and this particular aspect of receptor function, which can potentially be influenced by drug treatment, may in part explain the heterogeneous clinical response among canc

SUBMITTER: Coban O 

PROVIDER: S-EPMC4375452 | biostudies-literature | 2015 Mar

REPOSITORIES: biostudies-literature