Journal article
Prolonged RXFP1 and RXFP2 signaling can be explained by poor internalization and a lack of β-arrestin recruitment
GE Callander, WG Thomas, RAD Bathgate
American Journal of Physiology Cell Physiology | Published : 2009
Abstract
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 β-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 32P metabolically labeled cells were used ..
View full abstractGrants
Awarded by National Health and Medical Research Council of Australia
Funding Acknowledgements
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.