Receptor activity-modifying proteins differentially modulate the G protein-coupling efficiency of amylin receptors.

@article{Morfis2008ReceptorAP,
  title={Receptor activity-modifying proteins differentially modulate the G protein-coupling efficiency of amylin receptors.},
  author={Maria M. Morfis and Nanda Tilakaratne and Sebastian G B Furness and George D Christopoulos and Tim D. Werry and Arthur Christopoulos and Patrick M. Sexton},
  journal={Endocrinology},
  year={2008},
  volume={149 11},
  pages={
          5423-31
        }
}
Receptor activity-modifying proteins (RAMPs) 1, 2, and 3 are prototypic G protein-coupled receptor accessory proteins that can alter not only receptor trafficking but also receptor phenotype. Specific RAMP interaction with the calcitonin receptor (CTR) generates novel and distinct receptors for the peptide amylin; however, the role of RAMPs in receptor signaling is not understood. The current study demonstrates that RAMP interaction with the CTRa in COS-7 or HEK-293 cells leads to selective… CONTINUE READING
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The relaxin family peptide receptor 3 (RXFP3) activates ERK1/2 through a PKC dependent mechanism

  • ET Van der Westhuizen, TD Werry, PM Sexton, RJ Summers
  • Mol Pharmacol
  • 2007
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