Cdk5 targets active Src for ubiquitin-dependent degradation by phosphorylating Src(S75)

@article{Pan2011Cdk5TA,
  title={Cdk5 targets active Src for ubiquitin-dependent degradation by phosphorylating Src(S75)},
  author={Qu Pan and Fengyu Qiao and Chengjiang Gao and Benjamin Norman and Lance M. Optican and Peggy S. Zelenka},
  journal={Cellular and Molecular Life Sciences},
  year={2011},
  volume={68},
  pages={3425-3436}
}
The non-receptor tyrosine kinase Src is a critical regulator of cytoskeletal contraction, cell adhesion, and migration. In normal cells, Src activity is stringently controlled by Csk-dependent phosphorylation of Src(Y530), and by Cullin-5-dependent ubiquitinylation, which affects active Src(pY419) exclusively, leading to its degradation by the proteosome. Previous work has shown that Src activity is also limited by Cdk5, a proline-directed kinase, which has been shown to phosphorylate Src(S75… CONTINUE READING