β-Arrestin–Dependent Endocytosis of Proteinase-Activated Receptor 2 Is Required for Intracellular Targeting of Activated Erk1/2

@article{Defea2000ArrestinDependentEO,
  title={β-Arrestin–Dependent Endocytosis of Proteinase-Activated Receptor 2 Is Required for Intracellular Targeting of Activated Erk1/2},
  author={K Defea and Jonathan Zalevsky and Marie Thoma and Olivier D{\'e}ry and R Dyche Mullins and NigelW. Bunnett},
  journal={The Journal of Cell Biology},
  year={2000},
  volume={148},
  pages={1267 - 1282}
}
Recently, a requirement for beta-arrestin-mediated endocytosis in the activation of extracellular signal-regulated kinases 1 and 2 (ERK1/2) by several G protein-coupled receptors (GPCRs) has been proposed. However, the importance of this requirement for function of ERK1/2 is unknown. We report that agonists of Galphaq-coupled proteinase-activated receptor 2 (PAR2) stimulate formation of a multiprotein signaling complex, as detected by gel filtration, immunoprecipitation and immunofluorescence… CONTINUE READING
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