Structural basis for UBA-mediated dimerization of c-Cbl ubiquitin ligase.

@article{Kozlov2007StructuralBF,
  title={Structural basis for UBA-mediated dimerization of c-Cbl ubiquitin ligase.},
  author={Guennadi Kozlov and Pascal Peschard and Brandon G Zimmerman and Tong Lin and Tudor Moldoveanu and Nura Mansur-Azzam and Kalle Gehring and Morag Park},
  journal={The Journal of biological chemistry},
  year={2007},
  volume={282 37},
  pages={27547-55}
}
Ligand-induced down-regulation by the ubiquitin-protein ligases, c-Cbl and Cbl-b, controls signaling downstream from many receptor-tyrosine kinases (RTK). Cbl proteins bind to phosphotyrosine residues on activated RTKs to affect ligand-dependent ubiquitylation of these receptors targeting them for degradation in the lysosome. Both c-Cbl and Cbl-b contain a ubiquitin-associated (UBA) domain, which is important for Cbl dimerization and tyrosine phosphorylation; however, the mechanism of UBA… CONTINUE READING