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{{protein
{{infobox protein
|Name=Receptor activity-modifying protein 1 (RAMP1)
|Name=Receptor activity-modifying protein 1
|caption=
|caption=
|image=
|image=
|width=
|width=500px
|HGNCid=9843
|HGNCid=9843
|Symbol=RAMP1
|Symbol=[[RAMP1]]
|AltSymbols=
|AltSymbols=
|EntrezGene= 10267
|EntrezGene= 10267
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|LocusSupplementaryData=-37.1
|LocusSupplementaryData=-37.1
}}
}}
 
{{infobox protein
{{protein
|Name=Receptor activity-modifying protein 2
|Name=Receptor activity-modifying protein 2 (RAMP2)
|caption=
|caption=
|image=
|image=
|width=
|width=
|HGNCid= 9844
|HGNCid= 9844
|Symbol=RAMP2
|Symbol=[[RAMP2]]
|AltSymbols=
|AltSymbols=
|EntrezGene= 10266
|EntrezGene= 10266
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|LocusSupplementaryData=-21.1
|LocusSupplementaryData=-21.1
}}
}}
 
{{infobox protein
{{protein
|Name=Receptor activity-modifying protein 3
|Name=Receptor activity-modifying protein 1 (RAMP3)
|caption=
|caption=
|image=
|image=
|width=
|width=
|HGNCid= 9845
|HGNCid= 9845
|Symbol=RAMP3
|Symbol=[[RAMP3]]
|AltSymbols=
|AltSymbols=
|EntrezGene= 10268
|EntrezGene= 10268
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|LocusSupplementaryData=-p12
|LocusSupplementaryData=-p12
}}
}}
'''Receptor activity-modifying proteins''' ('''RAMPs''') are a class of protein that interact with and modulate the activities of several Class B [[GPCR|G protein-coupled receptor]]s including the receptors for [[secretin receptor|secretin]], [[calcitonin receptor|calcitonin]] (CT), [[glucagon receptor|glucagon]], and [[vasoactive intestinal peptide receptor|vasoactive intestinal peptide]] (VIP).<ref name="Sexton">{{cite journal |vauthors=Sexton PM, Morfis M, Tilakaratne N, Hay DL, Udawela M, Christopoulos G, Christopoulos A |title=Complexing receptor pharmacology: modulation of family B G protein-coupled receptor function by RAMPs|journal= Ann N Y Acad Sci |volume= 1070 |issue= |pages=90–104 |year= 2006 | pmid = 16888151 | doi=10.1196/annals.1317.076 }}</ref> There are three distinct types of RAMPs, designated [[RAMP1]], [[RAMP2]], and [[RAMP3]], each encoded by a separate gene.<ref name="Young">{{cite journal |author=Young A |title=Amylin: Physiology and Pharmacology; Chapter 3: Receptor pharmacology|journal=Advances in Pharmacology |volume= 52 |issue= |pages=47–65 |year= 2005 | pmid = 16492540 | doi = 10.1016/S1054-3589(05)52003-9 |series=Advances in Pharmacology |isbn=978-0-12-032954-0 }}</ref>
== Function ==
{{refimprove section|date=May 2009}}
Currently, the function of RAMPs is divided into classes of activities.  When associated with the [[Calcitonin receptor]] (CTR) or [[CALCRL|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 [[endoplasmic reticulum|ER]] / [[golgi apparatus|golgi]] to the membrane.  These functions appear to be ones where there is redundancy, as neither RAMP1 nor RAMP3 [[knockout mouse|knockout mice]] (KO) have grossly abnormal [[phenotype]]s.  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 [[calcitonin receptor|CT]] or [[CALCRL]] proteins forms 6 different receptors from the calcitonin receptor family:<ref name="IUPHAR-DB">*{{cite web | url = http://www.iuphar-db.org/GPCR/IntroductionDisplayForward?chapterID=1358 | title = Calcitonin Receptors: Introduction | accessdate = | author = | date = | work = IUPHAR Database of Receptors and Ion Channels | publisher = International Union of Basic and Clinical Pharmacology | pages = | archiveurl = | archivedate = }}</ref><ref name="pmid9620797">{{cite journal | vauthors = McLatchie LM, Fraser NJ, Main MJ, Wise A, Brown J, Thompson N, Solari R, Lee MG, Foord SM | title = RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor | journal = Nature | volume = 393 | issue = 6683 | pages = 333–9 |date=May 1998 | pmid = 9620797 | doi = 10.1038/30666 | url =  }}</ref><ref name="pmid10354609">{{cite journal | vauthors = Foord SM, Marshall FH | title = RAMPs: accessory proteins for seven transmembrane domain receptors | journal = Trends Pharmacol. Sci.| volume = 20 | issue = 5 | pages = 184–7 |date=May 1999 | pmid = 10354609 | doi = 10.1016/S0165-6147(99)01347-4 | url = }}</ref>
{| class="wikitable" border="1" style="text-align:center"
|-
! GPCR
! RAMP isoform
! resultant receptor
|-
| rowspan="3"|  [[CALCRL|Calcitonin receptor-like]]
| [[RAMP1]]
| [[CGRP]] receptor
|-
| [[RAMP2]]
| [[adrenomedullin]] (AM) receptor, designated AM<sub>1</sub><ref name="pmid10217420">{{cite journal | vauthors = Kamitani S, Asakawa M, Shimekake Y, Kuwasako K, Nakahara K, Sakata T | title = The RAMP2/CRLR complex is a functional adrenomedullin receptor in human endothelial and vascular smooth muscle cells | journal = FEBS Lett. | volume = 448 | issue = 1 | pages = 111–4 |date=April 1999 | pmid = 10217420 | doi = 10.1016/S0014-5793(99)00358-0  | url =  }}</ref>
|-
| [[RAMP3]]
| dual CGRP/AM receptor, designated AM<sub>2</sub>
|-
| rowspan="3"|  [[Calcitonin receptor]]
| RAMP1
| [[amylin]] receptor AMY<sub>1</sub>
|-
| RAMP2
| amylin receptor AMY<sub>2</sub>
|-
| RAMP3
| amylin receptor AMY<sub>3</sub>
|}


'''Receptor activity-modifying proteins''' ('''RAMP'''s) are a class of proteins which interact with and modulate the activities of several Class B [[GPCR|G Protein-Coupled Receptor]]s including the receptors for [[secretin receptor|secretin]], [[calcitonin receptor|calcitonin]] (CT), [[glucagon receptor|glucagon]], and [[vasoactive intestinal peptide receptor|vasoactive intestinal peptide]] (VIP).<ref name="Sexton">{{cite journal |author=Sexton PM, Morfis M, Tilakaratne N, Hay DL, Udawela M, Christopoulos G, Christopoulos A |title=Complexing receptor pharmacology: modulation of family B G protein-coupled receptor function by RAMPs|journal= Ann N Y Acad Sci |volume= 1070 |issue= |pages=90-104 |year= 2006 | pmid = 16888151}}</ref> There are three distinct types of RAMPs, designated '''RAMP1''', '''RAMP2''', and '''RAMP3''', each encoded by a separate gene.<ref name="Young">{{cite journal |author=Young A |title=Amylin: Physiology and Pharmacology; Chapter 3: Receptor pharmacology|journal=Advances in Pharmacology |volume= 52 |issue= |pages=47-65 |year= 2005 | pmid = 16492540}}</ref>
== References ==
{{Reflist}}


==External links==
==External links==
* {{cite web | url = http://www.iuphar-db.org/GPCR/ChapterMenuForward?chapterID=1358 | title = Calcitonin Receptors | accessdate = | author = | date = | work = IUPHAR Database of Receptors and Ion Channels | publisher = International Union of Basic and Clinical Pharmacology | pages = | archiveurl = | archivedate = }}
* {{MeshName|Receptor+activity+modifying+protein}}
* {{MeshName|Receptor+activity+modifying+protein}}


== References ==
{{Neuropeptide receptors}}
{{reflist|2}}<br />
{{Peptide receptor modulators}}
{{Growth factor receptor modulators}}
 


{{protein-stub}}
{{protein-stub}}
{{Neuropeptide receptors}}

Revision as of 00:58, 14 October 2017

Receptor activity-modifying protein 1
Identifiers
SymbolRAMP1
Entrez10267
HUGO9843
OMIM605153
RefSeqNM_005855
UniProtO60894
Other data
LocusChr. 2 q36-37.1
Receptor activity-modifying protein 2
Identifiers
SymbolRAMP2
Entrez10266
HUGO9844
OMIM605154
RefSeqNM_005854
UniProtO60895
Other data
LocusChr. 17 q12-21.1
Receptor activity-modifying protein 3
Identifiers
SymbolRAMP3
Entrez10268
HUGO9845
OMIM605155
RefSeqNM_005856
UniProtO60896
Other data
LocusChr. 7 q13-p12

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, 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.

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

  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.
  2. ↑ Young A (2005). "Amylin: Physiology and Pharmacology; Chapter 3: Receptor pharmacology". Advances in Pharmacology. Advances in Pharmacology. 52: 47–65. doi:10.1016/S1054-3589(05)52003-9. ISBN 978-0-12-032954-0. PMID 16492540.
  3. ↑ *"Calcitonin Receptors: Introduction". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology.
  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. doi:10.1038/30666. PMID 9620797.
  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.
  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. doi:10.1016/S0014-5793(99)00358-0. PMID 10217420.

External links


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