scholarly journals Molecular Basis of Association of Receptor Activity-Modifying Protein 3 with the Family B G Protein-Coupled Secretin Receptor

Biochemistry ◽  
2009 ◽  
Vol 48 (49) ◽  
pp. 11773-11785 ◽  
Author(s):  
Kaleeckal G. Harikumar ◽  
John Simms ◽  
George Christopoulos ◽  
Patrick M. Sexton ◽  
Laurence J. Miller
Keyword(s):  
G Protein ◽  
Molecular Basis ◽  
Receptor Activity ◽  
Secretin Receptor ◽  
The Family ◽  
G Protein Coupled

scholarly journals Functional Importance of a Structurally Distinct Homodimeric Complex of the Family B G Protein-Coupled Secretin Receptor

2009 ◽  
Vol 76 (2) ◽  
pp. 264-274 ◽  
Author(s):  
Fan Gao ◽  
Kaleeckal G. Harikumar ◽  
Maoqing Dong ◽  
Polo C.-H. Lam ◽  
Patrick M. Sexton ◽  
...  
Keyword(s):  
G Protein ◽  
Functional Importance ◽  
Secretin Receptor ◽  
The Family ◽  
G Protein Coupled

scholarly journals Adhesion GPCRs in Glioblastoma

2021 ◽  
Author(s):  
Gabriele Stephan ◽  
Niklas Ravn-Boess ◽  
Dimitris G Placantonakis
Keyword(s):  
G Protein ◽  
G Protein Coupled Receptors ◽  
The Past ◽  
Novel Treatment ◽  
The Family ◽  
Health And Disease ◽  
Basic Biology ◽  
G Protein Coupled ◽  
Potential Use ◽  
Receptor Family

Abstract Members of the adhesion family of G protein-coupled receptors (GPCRs) have received attention for their roles in health and disease, including cancer. Over the past decade, several members of the family have been implicated in the pathogenesis of glioblastoma. Here, we discuss the basic biology of adhesion GPCRs and review in detail specific members of the receptor family with known functions in glioblastoma. Finally, we discuss the potential use of adhesion GPCRs as novel treatment targets in neuro-oncology.

scholarly journals The molecular basis of subtype selectivity of human kinin G-protein-coupled receptors

2018 ◽  
Vol 14 (3) ◽  
pp. 284-290 ◽  
Author(s):  
Lisa Joedicke ◽  
Jiafei Mao ◽  
Georg Kuenze ◽  
Christoph Reinhart ◽  
Tejaswi Kalavacherla ◽  
...  
Keyword(s):  
G Protein ◽  
Molecular Basis ◽  
G Protein Coupled Receptors ◽  
Subtype Selectivity ◽  
G Protein Coupled

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

scholarly journals Structure of the Mouse Sex Peptide Pheromone ESP1 Reveals a Molecular Basis for Specific Binding to the Class C G-protein-coupled Vomeronasal Receptor

2013 ◽  
Vol 288 (22) ◽  
pp. 16064-16072 ◽  
Author(s):  
Sosuke Yoshinaga ◽  
Toru Sato ◽  
Makoto Hirakane ◽  
Kaori Esaki ◽  
Takashi Hamaguchi ◽  
...  
Keyword(s):  
G Protein ◽  
Molecular Basis ◽  
Specific Binding ◽  
Sex Peptide ◽  
Vomeronasal Receptor ◽  
Peptide Pheromone ◽  
Class C ◽  
G Protein Coupled

scholarly journals G-protein-coupled receptor 30 interacts with receptor activity-modifying protein 3 and confers sex-dependent cardioprotection

2013 ◽  
Vol 51 (1) ◽  
pp. 191-202 ◽  
Author(s):  
Patricia M Lenhart ◽  
Stefan Broselid ◽  
Cordelia J Barrick ◽  
L M Fredrik Leeb-Lundberg ◽  
Kathleen M Caron
Keyword(s):  
G Protein ◽  
Transmembrane Protein ◽  
Resonance Energy Transfer ◽  
Resonance Energy ◽  
Cardiac Cells ◽  
Receptor Activity ◽  
Hek293 Cells ◽  
G Protein Coupled

Receptor activity-modifying protein 3 (RAMP3) is a single-pass transmembrane protein known to interact with and affect the trafficking of several G-protein-coupled receptors (GPCRs). We sought to determine whether RAMP3 interacts with GPR30, also known as G-protein-coupled estrogen receptor 1. GPR30 is a GPCR that binds estradiol and has important roles in cardiovascular and endocrine physiology. Using bioluminescence resonance energy transfer titration studies, co-immunoprecipitation, and confocal microscopy, we show that GPR30 and RAMP3 interact. Furthermore, the presence of GPR30 leads to increased expression of RAMP3 at the plasma membrane in HEK293 cells. In vivo, there are marked sex differences in the subcellular localization of GPR30 in cardiac cells, and the hearts of Ramp3−/− mice also show signs of GPR30 mislocalization. To determine whether this interaction might play a role in cardiovascular disease, we treated Ramp3+/+ and Ramp3−/− mice on a heart disease-prone genetic background with G-1, a specific agonist for GPR30. Importantly, this in vivo activation of GPR30 resulted in a significant reduction in cardiac hypertrophy and perivascular fibrosis that is both RAMP3 and sex dependent. Our results demonstrate that GPR30–RAMP3 interaction has functional consequences on the localization of these proteins both in vitro and in vivo and that RAMP3 is required for GPR30-mediated cardioprotection.

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