| Receptor activity-modifying protein | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | RAMP | ||||||||
| Pfam | PF04901 | ||||||||
| InterPro | IPR006985 | ||||||||
| Membranome | 10 | ||||||||
| |||||||||
Receptor activity-modifying proteins (RAMPs) are a class of protein that interact with and modulate the activities of several Class B G protein-coupled receptors including the receptors for secretin, calcitonin (CT), glucagon, and vasoactive intestinal peptide (VIP).[1] There are three distinct types of RAMPs in mammals (though more in fish), designated RAMP1, RAMP2, and RAMP3, each encoded by a separate gene.[2]
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Transcription
Function
Currently, the function of RAMPs is divided into classes of activities. When associated with the Calcitonin receptor (CTR) or Calcitonin receptor-like (CALCRL) (below), RAMPs can change the selectivity of the receptor for a specific hormone. In the cases of the other receptors mentioned, however, there is no evidence that they can do this, but instead function to regulate trafficking of receptors from the ER / golgi to the membrane. These functions appear to be ones where there is redundancy, as neither RAMP1 nor RAMP3 knockout mice (KO) have grossly abnormal phenotypes. The likelihood is that the phenotype of RAMP2 KO mice is more connected with the abolition of most adrenomedullin (AM) signalling than effects on trafficking of other receptors, as those mice are almost identical to AM KO mice and mice lacking the Calcitonin-like receptor which are unable to form either AM1 or AM-2 adrenomedullin receptors (CLR/RAMP2 and CLR/RAMP3 respectively).
Types
Association of RAMPs with either the CT or CALCRL proteins forms 6 different receptors from the calcitonin receptor family:[3][4][5]
| GPCR | RAMP isoform | resultant receptor |
|---|---|---|
| Calcitonin receptor-like | RAMP1 | CGRP receptor |
| RAMP2 | adrenomedullin (AM) receptor, designated AM1[6] | |
| RAMP3 | dual CGRP/AM receptor, designated AM2 | |
| Calcitonin receptor | RAMP1 | amylin receptor AMY1 |
| RAMP2 | amylin receptor AMY2 | |
| RAMP3 | amylin receptor AMY3 |
References
- ^ Sexton PM, Morfis M, Tilakaratne N, Hay DL, Udawela M, Christopoulos G, Christopoulos A (2006). "Complexing receptor pharmacology: modulation of family B G protein-coupled receptor function by RAMPs". Ann N Y Acad Sci. 1070 (1): 90–104. Bibcode:2006NYASA1070...90S. doi:10.1196/annals.1317.076. PMID 16888151. S2CID 83595488.
- ^ Young A (2005). "Receptor Pharmacology". Amylin: Physiology and Pharmacology; Chapter 3: Receptor pharmacology. Advances in Pharmacology. Vol. 52. pp. 47–65. doi:10.1016/S1054-3589(05)52003-9. ISBN 978-0-12-032954-0. PMID 16492540.
- ^ *"Calcitonin Receptors: Introduction". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology. Archived from the original on 2016-03-03. Retrieved 2008-12-12.
- ^ McLatchie LM, Fraser NJ, Main MJ, Wise A, Brown J, Thompson N, Solari R, Lee MG, Foord SM (May 1998). "RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor". Nature. 393 (6683): 333–9. Bibcode:1998Natur.393..333M. doi:10.1038/30666. PMID 9620797. S2CID 4364526.
- ^ Foord SM, Marshall FH (May 1999). "RAMPs: accessory proteins for seven transmembrane domain receptors". Trends Pharmacol. Sci. 20 (5): 184–7. doi:10.1016/S0165-6147(99)01347-4. PMID 10354609.
- ^ Kamitani S, Asakawa M, Shimekake Y, Kuwasako K, Nakahara K, Sakata T (April 1999). "The RAMP2/CRLR complex is a functional adrenomedullin receptor in human endothelial and vascular smooth muscle cells". FEBS Lett. 448 (1): 111–4. Bibcode:1999FEBSL.448..111K. doi:10.1016/S0014-5793(99)00358-0. PMID 10217420. S2CID 23729715.
External links
- "Calcitonin Receptors". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology. Archived from the original on 2016-03-03. Retrieved 2008-12-12.
- Receptor+activity+modifying+protein at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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This page was last edited on 12 May 2024, at 16:16