Mechanism of Allosteric Coupling into and through the Plasma Membrane by EGFR.

ABSTRACT: Epidermal growth factor receptor (EGFR) interacts through its extracellular domain with seven different growth factors. These factors induce different structures within the cytoplasmic juxtamembrane (JM) segment of the dimeric receptor and propagate different growth factor-dependent signals to the cell interior. How this process occurs is unknown. Here we apply diverse experimental and computational tools to show that growth factor identity is encoded by the EGFR transmembrane (TM) helix into discrete helix dimer populations that differ in both cross-location and cross-angle. Helix dimers with smaller cross-angles at multiple cross locations are decoded to induce an EGF-type coiled coil in the adjacent JM, whereas helix dimers with larger cross-angles at fewer cross locations induce the TG

SUBMITTER: Sinclair JKL 

PROVIDER: S-EPMC6054568 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature