Phosphorylation of angiomotin by Lats1/2 kinases inhibits F-actin binding, cell migration, and angiogenesis.

@article{Dai2013PhosphorylationOA,
  title={Phosphorylation of angiomotin by Lats1/2 kinases inhibits F-actin binding, cell migration, and angiogenesis.},
  author={Xiaoming Dai and Peilu She and Fangtao Chi and Weifeng Ding and Huan Liu and Daqing Jin and Yiqiang Zhao and Xiaocan Guo and DanDan Jiang and Kun Liang Guan and Tao P. Zhong and Bin Zhao},
  journal={The Journal of biological chemistry},
  year={2013},
  volume={288 47},
  pages={34041-51}
}
The Hippo tumor suppressor pathway plays important roles in organ size control through Lats1/2 mediated phosphorylation of the YAP/TAZ transcription co-activators. However, YAP/TAZ independent functions of the Hippo pathway are largely unknown. Here we report a novel role of the Hippo pathway in angiogenesis. Angiomotin p130 isoform (AMOTp130) is phosphorylated on a conserved HXRXXS motif by Lats1/2 downstream of GPCR signaling. Phosphorylation disrupts AMOT interaction with F-actin and… CONTINUE READING