Insulin-induced beta-arrestin1 Ser-412 phosphorylation is a mechanism for desensitization of ERK activation by Galphai-coupled receptors.

@article{Hupfeld2005InsulininducedBS,
  title={Insulin-induced beta-arrestin1 Ser-412 phosphorylation is a mechanism for desensitization of ERK activation by Galphai-coupled receptors.},
  author={Christopher J. Hupfeld and Jamie L. Resnik and Satoshi Ugi and Jerrold M. Olefsky},
  journal={The Journal of biological chemistry},
  year={2005},
  volume={280 2},
  pages={1016-23}
}
Beta-arrestin1 is an adapter/scaffold for many G protein-coupled receptors during mitogen-activated protein kinase signaling. Phosphorylation of beta-arrestin1 at position Ser-412 is a regulator of beta-arrestin1 function, and in the present study, we showed that insulin led to a time- and dose-dependent increase in beta-arrestin1 Ser-412 phosphorylation, which blocked isoproterenol- and lysophosphatidic acid-induced Ser-412 dephosphorylation and impaired ERK signaling by these G protein… CONTINUE READING

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