scholarly journals Structure and Dynamics of Adrenomedullin Receptors AM1 and AM2 Reveal Key Mechanisms in the Control of Receptor Phenotype by Receptor Activity-Modifying Proteins

2020 ◽  
Vol 3 (2) ◽  
pp. 263-284 ◽  
Author(s):  
Yi-Lynn Liang ◽  
Matthew J. Belousoff ◽  
Madeleine M. Fletcher ◽  
Xin Zhang ◽  
Maryam Khoshouei ◽  
...  
Keyword(s):  
Receptor Activity ◽  
Structure And Dynamics ◽  
Receptor Activity Modifying Proteins ◽  
Receptor Phenotype

scholarly journals Receptor Activity-Modifying Proteins Differentially Modulate the G Protein-Coupling Efficiency of Amylin Receptors

Endocrinology ◽  
2008 ◽  
Vol 149 (11) ◽  
pp. 5423-5431 ◽  
Author(s):  
Maria Morfis ◽  
Nanda Tilakaratne ◽  
Sebastian G. B. Furness ◽  
George Christopoulos ◽  
Tim D. Werry ◽  
...  
Keyword(s):  
G Protein ◽  
Coupling Efficiency ◽  
Receptor Activity ◽  
G Protein Coupling ◽  
Hek 293 ◽  
Protein Coupling ◽  
Intracellular Ca ◽  
Fold Induction ◽  
Receptor Activity Modifying Proteins ◽  
Receptor Phenotype

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 signaling is not understood. The current study demonstrates that RAMP interaction with the CTRa in COS-7 or HEK-293 cells leads to selective modulation of signaling pathways activated by the receptor complex. There was a 20- to 30-fold induction in amylin potency at CTR/RAMP1 (AMY1) and CTR/RAMP3 (AMY3) receptors, compared with CTR alone, for formation of the second-messenger cAMP that parallels an increase in amylin binding affinity. In contrast, only 2- to 5-fold induction of amylin potency was seen for mobilization of intracellular Ca++ or activation of ERK1/2. In addition, in COS-7 cells, the increase in amylin potency for Ca++ mobilization was 2-fold greater for AMY3 receptors, compared with AMY1 receptors and this paralleled the relative capacity of overexpression of Gαq proteins to augment induction of high affinity 125I-amylin binding. These data demonstrate that RAMP-complexed receptors have a different signaling profile to CTRs expressed in the absence of RAMPs, and this is likely due to direct effects of the RAMP on G protein-coupling efficiency.

The effects of C-terminal truncation of receptor activity modifying proteins on the induction of amylin receptor phenotype from human CTb receptors

2008 ◽  
Vol 145 (1-3) ◽  
pp. 65-71 ◽  
Author(s):  
Madhara Udawela ◽  
George Christopoulos ◽  
Maria Morfis ◽  
Nanda Tilakaratne ◽  
Arthur Christopoulos ◽  
...  
Keyword(s):  
Receptor Activity ◽  
Receptor Activity Modifying Proteins ◽  
Receptor Phenotype

scholarly journals Receptor activity modifying proteins (RAMPs) interact with the VPAC2receptor and CRF1receptors and modulate their function

2013 ◽  
Vol 168 (4) ◽  
pp. 822-834 ◽  
Author(s):  
D Wootten ◽  
H Lindmark ◽  
M Kadmiel ◽  
H Willcockson ◽  
KM Caron ◽  
...  
Keyword(s):  
Receptor Activity ◽  
Receptor Activity Modifying Proteins

Receptor Activity Modifying Proteins Have Limited Effects on the Class B G Protein-Coupled Receptor Calcitonin Receptor-Like Receptor Stalk

Biochemistry ◽  
2018 ◽  
Vol 57 (8) ◽  
pp. 1410-1422 ◽  
Author(s):  
Michael L. Garelja ◽  
Christina A. Walker ◽  
Andrew Siow ◽  
Sung H. Yang ◽  
Paul W.R. Harris ◽  
...  
Keyword(s):  
G Protein ◽  
Receptor Activity ◽  
Calcitonin Receptor ◽  
G Protein Coupled Receptor ◽  
Class B ◽  
Receptor Activity Modifying Proteins ◽  
G Protein Coupled

Receptor activity modifying proteins

2001 ◽  
Vol 13 (2) ◽  
pp. 73-83 ◽  
Author(s):  
Patrick M Sexton ◽  
Anthony Albiston ◽  
Maria Morfis ◽  
Nanda Tilakaratne
Keyword(s):  
Receptor Activity ◽  
Receptor Activity Modifying Proteins
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