Receptor Activity-modifying Protein

Receptor activity-modifying protein 1
Receptor activity-modifying protein 1
Identifiers
Symbol	RAMP1
NCBI gene	10267
HGNC	9843
OMIM	605153
RefSeq	NM_005855
UniProt	O60894
Other data
Locus	Chr. 2 q36-37.1
Structures
Search for
Structures	Swiss-model
Domains	InterPro

Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Receptor activity-modifying protein
Receptor activity-modifying protein
Identifiers
Symbol	RAMP
Pfam	PF04901
InterPro	IPR006985
Membranome	10
Pfam
Available protein structures:
Pfam	structures / ECOD
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Receptor activity-modifying protein 2

Identifiers

Symbol

Other data

Chr. 17 q12-21.1

Search for
Structures	Swiss-model
Domains	InterPro

Receptor activity-modifying protein 3

Identifiers

Symbol

Other data

Chr. 7 q13-p12

Search for
Structures	Swiss-model
Domains	InterPro

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]

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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[Sexton-1] 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-2] 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.

[IUPHAR-DB-3] * "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.

[pmid9620797-4] 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.

[pmid10354609-5] 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.

[pmid10217420-6] 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.

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