Prolonged RXFP1 and RXFP2 signaling can be explained by poor internalization and a lack of beta-arrestin recruitment
Gabrielle E Callander, Walter G Thomas, Ross AD Bathgate
AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY | AMER PHYSIOLOGICAL SOC | Published : 2009
Relaxin induces sustained physiological responses, which brings into question the deactivation processes typical of most G protein-coupled receptors (GPCR) for its receptor, relaxin family peptide receptor 1 (RXFP1). Here, we examined relaxin-dependent phosphorylation of RXFP1 and the related insulin-like peptide 3 (INSL3) receptor, RXFP2, as well as the capacity of these receptors to recruit beta-arrestins and internalize in response to ligand stimulation. We confirmed in human embryonic kidney (HEK)-293T cells, expressing RXFP1 or RXFP2, that both receptors elicit prolonged cAMP responses up to 6 h after stimulation. Receptors immunoprecipitated from (32)P metabolically labeled cells were ..View full abstract
Awarded by National Health and Medical Research Council of Australia
This work was supported by Project Grants 300012 (to R. A. D. Bathgate) and 418921 (to W. G. Thomas) from the National Health and Medical Research Council of Australia.