ABSTRACT
Signaling by transmembrane receptors involves the coordinated assembly of macromolecular complexes under constraints imposed by the organization of the plasma membrane (PM). Signaling by receptor tyrosine kinases (RTKs) such as the epidermal growth factor receptor (EGFR or erbB1) or macrophage colony-stimulating factor receptor (MCSFR) requires rearrangements on the PM including receptor dimerization, phosphorylation, signaling complex assembly, and endocytosis (Figure 12.1).1,2 While the protein-protein interactions of RTK signal transduction have been extensively studied, the contributions of the PM in controlling the diffusion and local concentrations of signaling components and therefore the dynamics of assembly and signal amplitudes remain poorly dened. Specically, how do the chemical potentials that modulate the lateral diffusion in the PM inuence receptor assembly?
