A small pool of active epidermal growth factor (EGF) receptors, which are capable of ubiquitylation and efficient endocytosis in vivo, is sufficient to support EGF-receptor-dependent tumor growth by signaling primarily through the Ras-MAPK pathway.

CRISPR/Cas9 gene-editing was used to generate a novel endogenous pH-sensitive EGF receptor chimera with the unique utility to study receptor endocytosis in a single-cell and high-throughput experimental formats.

Preferential endocytosis of activated receptors allows cells to memorize their past and perform relative sensing.

Cells package active receptors in endosomes at fairly constant amounts and can determine different cell-fate decisions by regulating the number and lifetime of receptor packages.

The co-chaperone CHORDC1 is specifically required for epidermal growth factor receptor trafficking and signaling in Caenorhabditis elegans and in human cells.

The recruitment of SH2-containing proteins to Epidermal Growth Factor in cells happens more slowly than predicted by in vitro techniques.

Unidirectional crosstalk occurs between signaling competent EGFR dimers activating RON within heteromeric complexes at the plasma membrane.

The transfer of O-GlcNAc by EOGT to specific EGF repeats of NOTCH1 promotes DLL4 binding, Notch signaling, and retinal vascular development.

Ligand capture by cell surface receptor complexes sets the shape of the Nodal signaling pattern in zebrafish.

Plasticity arising from autocatalytic receptor activation coexists with robustness in ligand responsiveness only by differential endosomal sorting of spontaneous and ligand-activated EGFR as distinct molecular states.