Epidermal growth factor receptor signaling intensity determines intracellular protein interactions, ubiquitination, and internalization.

@article{Schmidt2003EpidermalGF,
  title={Epidermal growth factor receptor signaling intensity determines intracellular protein interactions, ubiquitination, and internalization.},
  author={Mirko H. H. Schmidt and Frank B Furnari and Webster K Cavenee and Oliver B{\"o}gler},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2003},
  volume={100 11},
  pages={
          6505-10
        }
}
Ligand activation of the epidermal growth factor receptor (EGFR) causes the binding of Cbls, which leads to EGFR polyubiquitination and internalization through endophilin complexes that contain the adaptor protein SH3-domain encoding, expressed in tumorigenic astrocytes/Cbl-interacting protein of 85 kDa/regulator of ubiquitous kinase (SETA/CIN85/Ruk). In cells grown at high density, high levels of SETA interfered in the recruitment of Casitas B-lineage (Cbl) proteins to the EGFR and reduced its… CONTINUE READING