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J. Biol. Chem., Vol. 278, Issue 5, 3293-3297, January 31, 2003
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From the The receptor activity-modifying proteins (RAMPs)
comprise a family of three accessory proteins that heterodimerize with
the calcitonin receptor-like receptor (CL receptor) or with the
calcitonin receptor (CTR) to generate different receptor phenotypes.
However, RAMPs are more widely distributed across cell and tissue types than the CTR and CL receptor, suggesting additional roles for RAMPs in
cellular processes. We have investigated the potential for RAMP
interaction with a number of Class II G protein-coupled receptors
(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 additional receptors, the
VPAC1 vasoactive intestinal polypeptide/pituitary adenylate
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 RAMPs with the CL
receptor or the CTR, VPAC1R-RAMP complexes do not show 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 enhancement of agonist-mediated
phosphoinositide hydrolysis with no change in cAMP stimulation
compared with the VPAC1R alone. Our findings identify a new
functional consequence of RAMP-receptor interaction, suggesting that
RAMPs play a more general role in modulating cell signaling through
other GPCRs than is currently appreciated.
Novel Receptor Partners and Function of Receptor
Activity-modifying Proteins*
§¶,
,,
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
*
This work was funded by National Health and Medical Research
Council (NHMRC) Grants 990024 and 145702.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
A senior research fellow of the National Health and Medical
Research Council of Australia. To whom correspondence should be addressed. Tel.: 61-3-8344-7334; Fax: 61-3-9348-1707; E-mail: p.sexton@hfi.unimelb.edu.au.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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