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Originally published In Press as doi:10.1074/jbc.M005604200 on July 19, 2000

J. Biol. Chem., Vol. 275, Issue 40, 31438-31443, October 6, 2000
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CGRP-RCP, a Novel Protein Required for Signal Transduction at Calcitonin Gene-related Peptide and Adrenomedullin Receptors*

Bornadata N. EvansDagger , Mark I. Rosenblatt§, Laila O. Mnayer§, Kevin R. Oliver, and Ian M. DickersonDagger §**

From the Departments of Dagger  Physiology and Biophysics, § Biochemistry and Molecular Biology, and ** Neuroscience Program, University of Miami School of Medicine, Miami, Florida 33101 and  Merck, Sharp and Dohme Research Laboratories, Neuroscience Research Center, Terling's Park, Harlow, Essex CM20 2QR, United Kingdom

It is becoming clear that receptors that initiate signal transduction by interacting with G-proteins do not function as monomers, but often require accessory proteins for function. Some of these accessory proteins are chaperones, required for correct transport of the receptor to the cell surface, but the function of many accessory proteins remains unknown. We determined the role of an accessory protein for the receptor for calcitonin gene-related peptide (CGRP), a potent vasodilator neuropeptide. We have previously shown that this accessory protein, the CGRP-receptor component protein (RCP), is expressed in CGRP responsive tissues and that RCP protein expression correlates with the biological efficacy of CGRP in vivo. However, the function of RCP has remained elusive. In this study stable cell lines were made that express antisense RCP RNA, and CGRP- and adrenomedullin-mediated signal transduction were greatly reduced. However, the loss of RCP did not effect CGRP binding or receptor density, indicating that RCP did not behave as a chaperone but was instead coupling the CGRP receptor to downstream effectors. A candidate CGRP receptor named calcitonin receptor-like receptor (CRLR) has been identified, and in this study RCP co-immunoprecipitated with CRLR indicating that these two proteins interact directly. Since CGRP and adrenomedullin can both signal through CRLR, which has been previously shown to require a chaperone protein for function, we now propose that a functional CGRP or adrenomedullin receptor consists of at least three proteins: the receptor (CRLR), the chaperone protein (RAMP), and RCP that couples the receptor to the cellular signal transduction pathway.

* This work was supported in part by National Institutes of Health Grant DK52328, American Heart Association (AHA) (Florida affiliate) Grant 9810018FL (to I. M. D.), AHA Post-doctoral Fellowship 9920180V (to B. N. E.), and AHA Pre-doctoral Fellowship 9804169V (to L. O. M.).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.

** To whom correspondence should be addressed: University of Miami School of Medicine, Dept. of Physiology and Biophysics, P. O. Box 016430, Miami, FL 33101. Tel.: 305-243-1280; Fax: 305-243-5931; E-mail: imd@miami.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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