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Receptor activity-modifying protein

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Receptor activity-modifying protein 1
Identifiers
SymbolRAMP1
NCBI gene10267
HGNC9843
OMIM605153
RefSeqNM_005855
UniProtO60894
Other data
LocusChr. 2 q36-37.1
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StructuresSwiss-model
DomainsInterPro

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Receptor activity-modifying protein 2
Identifiers
SymbolRAMP2
NCBI gene10266
HGNC9844
OMIM605154
RefSeqNM_005854
UniProtO60895
Other data
LocusChr. 17 q12-21.1
Search for
StructuresSwiss-model
DomainsInterPro

Template:FixBunching

Receptor activity-modifying protein 3
Identifiers
SymbolRAMP3
NCBI gene10268
HGNC9845
OMIM605155
RefSeqNM_005856
UniProtO60896
Other data
LocusChr. 7 q13-p12
Search for
StructuresSwiss-model
DomainsInterPro

Template:FixBunching Receptor activity-modifying proteins (RAMPs) are a class of protein which 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, designated RAMP1, RAMP2, and RAMP3, each encoded by a separate gene.[2]

Function

Currently the function of RAMPs is divided into two activities. When associated with the CTR or 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 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.

Types

Association of RAMPs with either the CT or CALCRL proteins form 6 different receptors from the calcitonin receptor family:[3][4][5]

GPCR RAMP isoform resultant receptor
Calcitonin receptor-like RAMP1 CGRP
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

  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: 90–104. doi:10.1196/annals.1317.076. PMID 16888151.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  2. ^ Young A (2005). "Amylin: Physiology and Pharmacology; Chapter 3: Receptor pharmacology". Advances in Pharmacology. 52: 47–65. doi:10.1016/S1054-3589(05)52003-9. PMID 16492540.
  3. ^ *"Calcitonin Receptors: Introduction". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology. {{cite web}}: Cite has empty unknown parameter: |coauthors= (help)
  4. ^ McLatchie LM, Fraser NJ, Main MJ, Wise A, Brown J, Thompson N, Solari R, Lee MG, Foord SM (1998). "RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor". Nature. 393 (6683): 333–9. doi:10.1038/30666. PMID 9620797. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)
  5. ^ Foord SM, Marshall FH (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. {{cite journal}}: Unknown parameter |month= ignored (help)
  6. ^ Kamitani S, Asakawa M, Shimekake Y, Kuwasako K, Nakahara K, Sakata T (1999). "The RAMP2/CRLR complex is a functional adrenomedullin receptor in human endothelial and vascular smooth muscle cells". FEBS Lett. 448 (1): 111–4. doi:10.1016/S0014-5793(99)00358-0. PMID 10217420. {{cite journal}}: Unknown parameter |month= ignored (help)CS1 maint: multiple names: authors list (link)