Feedback regulation of beta-arrestin1 function by extracellular signal-regulated kinases.

@article{Lin1999FeedbackRO,
  title={Feedback regulation of beta-arrestin1 function by extracellular signal-regulated kinases.},
  author={Fang Ting Lin and William E Miller and Louis M Luttrell and Robert J Lefkowitz},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 23},
  pages={
          15971-4
        }
}
The functions of beta-arrestin1 to facilitate clathrin-mediated endocytosis of the beta2-adrenergic receptor and to promote agonist-induced activation of extracellular signal-regulated kinases (ERK) are regulated by its phosphorylation/dephosphorylation at Ser-412. Cytoplasmic beta-arrestin1 is almost stoichiometrically phosphorylated at Ser-412. Dephosphorylation of beta-arrestin1 at the plasma membrane is required for targeting a signaling complex that includes the agonist-occupied receptors… CONTINUE READING
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