An elegant dissection of how EGFR activation depends on conformational coupling across the plasma membrane, revealing that ligand binding, transmembrane helix dimerization, and juxtamembrane interactions are essential to overcoming membrane-imposed inhibition and stabilizing the active kinase dimer.
A deep dive into the molecular dynamics and membrane interaction of EGFR, revealing distinct active and inactive conformations, the role of lipid environment, and subtle structural regulation.
A deep dive into the molecular dynamics and membrane interaction of EGFR, revealing distinct active and inactive conformations, the role of lipid environment, and subtle structural regulation.
An in-depth study of EGFR activation focusing on transmembrane and juxtamembrane coupling, density-dependent activation, and the role of the plasma membrane in maintaining autoinhibition.
An in-depth study of EGFR activation focusing on transmembrane and juxtamembrane coupling, density-dependent activation, and the role of the plasma membrane in maintaining autoinhibition.
A study demonstrating that EGFR activation is not tightly coupled to specific transmembrane dimerization interfaces, suggesting a loose linkage between extracellular ligand binding and intracellular kinase activation.
A study demonstrating that EGFR activation is not tightly coupled to specific transmembrane dimerization interfaces, suggesting a loose linkage between extracellular ligand binding and intracellular kinase activation.
Notes on the 2021 Nature Communications paper revealing a calcium-dependent APPL1-dynein mechanism that coordinates collective EGFR trafficking to the perinuclear region following stimulation.
Notes on the 2021 Nature Communications paper revealing a calcium-dependent APPL1-dynein mechanism that coordinates collective EGFR trafficking to the perinuclear region following stimulation.
