Src-dependent tyrosine phosphorylation regulates dynamin self-assembly and ligand-induced endocytosis of the epidermal growth factor receptor.

@article{Ahn2002SrcdependentTP,
  title={Src-dependent tyrosine phosphorylation regulates dynamin self-assembly and ligand-induced endocytosis of the epidermal growth factor receptor.},
  author={Seungkirl Ahn and Jihee Kim and Carmen L Lucaveche and Mary C. Reedy and Louis M. Luttrell and Robert J Lefkowitz and Yehia Daaka},
  journal={The Journal of biological chemistry},
  year={2002},
  volume={277 29},
  pages={26642-51}
}
Endocytosis of ligand-activated receptors requires dynamin-mediated GTP hydrolysis, which is regulated by dynamin self-assembly. Here, we demonstrate that phosphorylation of dynamin I by c-Src induces its self-assembly and increases its GTPase activity. Electron microscopic analyses reveal that tyrosine-phosphorylated dynamin I spontaneously self-assembles into large stacks of rings. Tyrosine 597 was identified as being phosphorylated both in vitro and in cultured cells following epidermal… CONTINUE READING