Receptor activity-modifying proteins differentially modulate the G protein-coupling efficiency of amylin receptors. [PDF]
Receptor activity-modifying proteins (RAMPs) 1, 2, and 3 are prototypic G protein-coupled receptor accessory proteins that can alter not only receptor trafficking but also receptor phenotype. Specific RAMP interaction with the calcitonin receptor (CTR) generates novel and distinct receptors for the peptide amylin; however, the role of RAMPs in receptor
M. Morfis +6 more
semanticscholar +3 more sources
Receptor activity-modifying proteins; multifunctional G protein-coupled receptor accessory proteins.
Receptor activity-modifying proteins (RAMPs) are single pass membrane proteins initially identified by their ability to determine the pharmacology of the calcitonin receptor-like receptor (CLR), a family B G protein-coupled receptor (GPCR). It is now known that RAMPs can interact with a much wider range of GPCRs.
D. Hay +5 more
semanticscholar +4 more sources
Regulation of the chemokine receptors CXCR4 and ACKR3 by receptor activity-modifying proteins. [PDF]
The chemokine CXCL12 and its two cognate receptors-CXCR4 and ACKR3-are key players in various homeostatic and pathophysiological processes, including embryonic development, autoimmune diseases, tissue repair, and cancer. Recent reports identified an interaction of CXCR4 and ACKR3 with receptor activity-modifying proteins (RAMPs), and RAMP3 has been ...
Pfersdorf F +3 more
europepmc +5 more sources
Receptor activity-modifying proteins: RAMPing up adrenomedullin signaling. [PDF]
Adrenomedullin (AM) is a 52-amino-acid multifunctional peptide that circulates in the plasma in the low picomolar range and can exert a multitude of biological effects through an autocrine/paracrine mode of action. The mechanism by which AM transduces its signal represents a novel and pharmacologically tractable paradigm in G protein-coupled receptor ...
C. Gibbons +4 more
semanticscholar +3 more sources
Erratum: An allosteric role for receptor activity-modifying proteins in defining GPCR pharmacology. [PDF]
Correction to: Cell Discovery (2016) 2, 16012; doi:10.1038/celldisc.2016.12; published online 17 May 2016 During web production, there was an error in Supplementary information: Supplementary Material was omitted. The files are now installed in the online version of the paper. We apologize for any inconvenience that may have been caused by this error.
Gingell JJ +7 more
europepmc +7 more sources
Novel Function for Receptor Activity-modifying Proteins (RAMPs) in Post-endocytic Receptor Trafficking*♦ [PDF]
RAMPs (1–3) are single transmembrane accessory proteins crucial for plasma membrane expression, which also determine receptor phenotype of various G-protein-coupled receptors.
J. Bomberger +4 more
semanticscholar +3 more sources
Visualization of the Calcitonin Receptor-like Receptor and Its Receptor Activity-modifying Proteins during Internalization and Recycling* [PDF]
Expression of the calcitonin receptor-like receptor (CRLR) and its receptor activity modifying proteins (RAMPs) can produce calcitonin gene-related peptide (CGRP) receptors (CRLR/RAMP1) and adrenomedullin (AM) receptors (CRLR/RAMP2 or -3).
K. Kuwasako +8 more
semanticscholar +3 more sources
Adrenomedullin selectivity of calcitonin-like receptor/receptor activity modifying proteins.
Co-expression of an initially orphan calcitonin receptor-like (CL)1 receptor with individual receptor-activity-modifying proteins (RAMP)1, -2 and -3 results in CL receptor/RAMP1, -2 and -3 proteins at the cell surface. The RAMP define the selectivity of the CL receptor for the vasodilatory peptides adrenomedullin (AM) and calcitonin gene-related ...
R. Muff, W. Born, J. Fischer
semanticscholar +3 more sources
Objectives: Receptor Activity-Modifying Protein 2 (RAMP2) is a chaperone protein which allosterically binds to and interacts with the glucagon receptor (GCGR).
Emma Rose McGlone +8 more
doaj +2 more sources
Receptor activity modifying proteins (RAMPs) interact with the VPAC2 receptor and CRF1 receptors and modulate their function. [PDF]
Wootten D +7 more
europepmc +2 more sources

