Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2006-8-4
pubmed:abstractText
The most well-characterized subgroup of family B G protein-coupledreceptors (GPCRs) comprises receptors for peptide hormones, such as secretin, calcitonin (CT), glucagon, and vasoactive intestinal peptide (VIP). Recent data suggest that many of these receptors can interact with a novel family of GPCR accessory proteins termed receptor activity modifying proteins (RAMPs). RAMP interaction with receptors can lead to a variety of actions that include chaperoning of the receptor protein to the cell surface as is the case for the calcitonin receptor-like receptor (CLR) and the generation of novel receptor phenotypes. RAMP heterodimerization with the CLR and related CT receptor is required for the formation of specific CT gene-related peptide, adrenomedullin (AM) or amylin receptors. More recent work has revealed that the specific RAMP present in a heterodimer may modulate other functions such as receptor internalization and recycling and also the strength of activation of downstream signaling pathways. In this article we review our current state of knowledge of the consequence of RAMP interaction with family B GPCRs.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0077-8923
pubmed:author
pubmed:issnType
Print
pubmed:volume
1070
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
90-104
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2006
pubmed:articleTitle
Complexing receptor pharmacology: modulation of family B G protein-coupled receptor function by RAMPs.
pubmed:affiliation
Howard Florey Institute, Level 2, Alan Gilbert Building, The University of Melbourne, 161 Barry Street, Carlton South, 3053, Victoria, Australia. p.sexton@hfi.unimelb.edu.au
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't