Binding of Cbl to a phospholipase Cgamma1-docking site on platelet-derived growth factor receptor beta provides a dual mechanism of negative regulation.

@article{Reddi2007BindingOC,
  title={Binding of Cbl to a phospholipase Cgamma1-docking site on platelet-derived growth factor receptor beta provides a dual mechanism of negative regulation.},
  author={Alagarsamy Lakku Reddi and Guoguang Ying and Lei Duan and Gengsheng Chen and Manjari Dimri and Patrice Douillard and Brian J. Druker and Mayumi Naramura and Vimla Band and Hamid Band},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 40},
  pages={29336-47}
}
Ubiquitin conjugation to receptor tyrosine kinases is a critical biochemical step in attenuating their signaling through lysosomal degradation. Our previous studies have established Cbl as an E3 ubiquitin ligase for ubiquitinylation and degradation of platelet-derived growth factor receptor (PDGFR) alpha and PDGFRbeta. However, the role of endogenous Cbl in PDGFR regulation and the molecular mechanisms of this regulation remain unclear. Here, we demonstrate that endogenous Cbl is essential for… CONTINUE READING

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