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Novel Receptor Partners and Function of Receptor
From the Department of Pharmacology and the
§ Howard Florey Institute, The University of Melbourne,
Victoria 3010, Australia, the Department of
Neuroendocrinology and Cell Biology, INSERM U410, Faculté de
Médecine Xavier Bichat, 75018, Paris, France, and the
** First Department of Internal Medicine, Miyazaki
Medical College, Miyazaki 889-1692, Japan
The receptor activity-modifying proteins (RAMPs)
comprise a family of three accessory proteins that heterodimerize with
thecalcitonin receptor-like receptor (CL receptor) or with the
calcitoninreceptor (CTR) to generate different receptor phenotypes.
However,RAMPs are more widely distributed across cell and tissue typesthan the CTR and CL receptor, suggesting additional roles forRAMPs in
cellular processes. We have investigated the potentialfor RAMP
interaction with a number of Class II G protein-coupledreceptors
(GPCRs) in addition to the CL receptor and the CTR.Using
immunofluorescence confocal microscopy, we demonstrate,for the first
time, that RAMPs interact with at least four additionalreceptors, the
VPAC1 vasoactive intestinal polypeptide/pituitaryadenylate
cyclase-activating peptide receptor with all three RAMPs;the
glucagon and PTH1 parathyroid hormone receptors with RAMP2;and the
PTH2 receptor with RAMP3. Unlike the interaction of RAMPswith the CL
receptor or the CTR, VPAC1R-RAMP complexes do notshow altered
phenotypic behavior compared with the VPAC1R alone,as determined using
radioligand binding in COS-7 cells. However,the VPAC1R-RAMP2
heterodimer displays a significant enhancementof agonist-mediated
phosphoinositide hydrolysis with no changein cAMP stimulation
compared with the VPAC1R alone. Our findingsidentify a new
functional consequence of RAMP-receptor interaction,suggesting that
RAMPs play a more general role in modulating cellsignaling through
other GPCRs than is currentlyappreciated.
G-protein-coupled receptor 30 interacts with receptor activity-modifying protein 3 and confers sex-dependent cardioprotection.
P. M. Lenhart, S. Broselid, C. J. Barrick, L. M. F. Leeb-Lundberg, and K. M. Caron (2013)
J. Mol. Endocrinol.
|Abstract »|Full Text »|PDF »
Regulation of myofibroblast differentiation and bleomycin-induced pulmonary fibrosis by adrenomedullin.
J. Kach, N. Sandbo, N. Sethakorn, J. Williams, E. B. Reed, J. La, X. Tian, S. D. Brain, K. Rajendran, R. Krishnan, et al. (2013)
Am J Physiol Lung Cell Mol Physiol
|Abstract »|Full Text »|PDF »
Adrenomedullin and calcitonin gene-related peptide receptors in endocrine-related cancers: opportunities and challenges.