Journal of Biological Chemistry · 1999 · 315 citations · 43 references
Life SciencesCell BiologyMolecular BiologyCell SignalingMembrane TraffickingSignal TransductionCell MigrationCell-surface ReceptorsGrowth Factor SignalingIntracellular ReceptorsMembrane ReceptorsReceptor RegulationClathrin-coated VesiclesEpidermal Growth Factor Receptor EndocytosisEpidermal Growth Factor Receptor SignalingGrowth Factor Receptor TraffickingMembrane Domain DynamicsOncogenic TransformationReceptor Tyrosine Kinase ActivationSignal Transduction At Caveolae
In quiescent fibroblasts, epidermal growth factor (EGF) receptors (EGFR) are initially concentrated in caveolae but rapidly move out of this membrane domain in response to EGF. To better understand the dynamic localization of EGFR to caveolae, we have studied the behavior of wild-type and mutant receptors expressed in cells lacking endogenous EGFR. All of the receptors we examined, including those missing the first 274 amino acids or most of the cytoplasmic tail, were constitutively concentrated in caveolae. By contrast, migration from caveolae required EGF binding, an active receptor kinase domain, and at least one of the five tyrosine residues present in the regulatory domain of the receptor. Movement appears to be modulated by Src kinase, is blocked by activators of protein kinase C, and occurs independently of internalization by clathrin-coated pits. Two mutant receptors previously shown to induce an oncogenic phenotype lack the ability to move from caveolae in response to EGF, suggesting that a prolonged residence in this domain may contribute to abnormal cell behavior.
43
Induction of mutant dynamin specifically blocks endocytic coated vesicle formation.
Hanna Damke, Toru Baba, Dale E. Warnock et al. · The Journal of Cell Biology · 1994 · 1.2K citations · Full text
A role for Pyk2 and Src in linking G-protein-coupled receptors with MAP kinase activation
George Tokiwa, Sima Lev, Sara A. Courtneidge et al. · Nature · 1996 · 972 citations