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 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 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 Two Novel Compound Heterozygous ADGRG1/GPR56 Mutations Associated with Diffuse Cerebral Polymicrogyria

2020 ◽  
Author(s):  
Ruchika Jha ◽  
Uday B. Kovilapu ◽  
Amit Devgan ◽  
Vishal Sondhi
Keyword(s):  
G Protein ◽  
Intractable Epilepsy ◽  
Brain Magnetic Resonance Imaging ◽  
Subsequent Pregnancy ◽  
Compound Heterozygous ◽  
G Protein Coupled Receptor ◽  
The Family ◽  
Occipital Lobes ◽  
G Protein Coupled ◽  
Spastic Quadriparesis

Abstract Background Polymicrogyria (PMG) has environmental or genetic etiologies. We report a 8-year-old boy with diffuse PMG and two novel adhesion G protein-coupled receptor G1 (ADGRG1)/G protein-coupled receptor 56 (GPR56) mutations. Case Report The proband has intellectual disability, spastic quadriparesis, and intractable epilepsy without antenatal or perinatal insults. Brain magnetic resonance imaging revealed PMG involving fronto-polar, parietal and occipital lobes with decreasing antero-posterior gradient, and a thinned-out brain stem. Targeted exome sequencing identified two novel compound heterozygote ADGRG1/GPR56 mutations (c.C209T and c.1010dupT), and each parent carries one of these mutations. Subsequent pregnancy was terminated because the fetus had the same mutations. Conclusion The detected mutations expanded the genetic etiology of PMG and helped the family to avoid another child with this devastating condition.

scholarly journals The secretin G-protein-coupled receptor family: teleost receptors

2005 ◽  
Vol 34 (3) ◽  
pp. 753-765 ◽  
Author(s):  
J C R Cardoso ◽  
M S Clark ◽  
F A Viera ◽  
P D Bridge ◽  
A Gilles ◽  
...  
Keyword(s):  
Vasoactive Intestinal Peptide ◽  
G Protein ◽  
Strong Support ◽  
Duplicated Genes ◽  
Related Peptide ◽  
Fugu Genome ◽  
The Family ◽  
Genome Consortium ◽  
G Protein Coupled ◽  
Receptor Family

Twenty-one members of the secretin family (family 2) of G-protein-coupled receptors (GPCRs) were identified via directed cloning and data-mining of the Fugu Genome Consortium database, representing the most comprehensive description of secretin GPCRs in a teleost fish to date. Duplicated genes were identified for many of the family members, namely the receptors for pituitary adenylate cyclase-activating polypeptide (PACAP)/vasoactive intestinal peptide (VIP), calcitonin, calcitonin gene-related peptide (CGRP), growth hormone releasing hormone (GHRH), glucagon receptor/glucagon-like peptide (GLP) and parathyroid hormone-related peptide (PTHrP)/PTH. Mining of other teleost genomes (zebrafish and Tetraodon) revealed that the duplicated genes identified in the Takifugu genome were also present in these fish. Additional database searching of the Escherichia coli, yeast, Drosophila, Caenorhabditis elegans and Ciona genomes revealed that the family 2 of GPCRs were only present in the multicellular organisms. Orthologues of all the human secretin receptors were identified with the exception of secretin itself. Additional database searches in the Fugu Genome Consortium database also failed to reveal a secretin ligand and so it is hypothesised that both the receptor and the ligand evolved after the divergence of teleost/tetrapod lineages. Phylogenetic analysis at both the protein and the DNA level provided strong support for each of the individual receptor family groupings, but weak support between groups, making evolutionary inferences difficult. A more critical analysis of the PACAP/VIP receptor family confirmed previous hypotheses that the vasoactive intestinal peptide receptor (VPAC1R) gene is the ancestral form of the receptor.

The orthosteric agonist-binding pocket in the prototypic class B G-protein-coupled secretin receptor

2013 ◽  
Vol 41 (1) ◽  
pp. 154-158 ◽  
Author(s):  
Laurence J. Miller ◽  
Maoqing Dong
Keyword(s):  
G Protein ◽  
Fluorescence Analysis ◽  
Binding Pocket ◽  
Rational Development ◽  
Secretin Receptor ◽  
Natural Ligands ◽  
Class B ◽  
G Protein Coupled ◽  
Moderate Length ◽  
Activity Series

Class B GPCRs (G-protein-coupled receptors) share heptahelical topology and G-protein binding with other superfamily members, yet have unique structures and modes of activation. Natural ligands for these receptors are moderate-length peptides with C-terminal α-helices. NMR and crystal structures of the peptide-bound disulfide-bonded receptor N-terminal domains demonstrate that these helices occupy a conserved groove; however, the details of this interaction vary from one receptor to another. In this review, we focus on the prototypic secretin receptor and use extensive intrinsic photoaffinity labelling, structure–activity series, alanine-replacement mutagenesis and fluorescence analysis to define the molecular basis for this interaction. Additionally, experimental validation of predictions coming from in silico molecular modelling has provided a basis for enhancement of binding affinity. Such insights will be useful in the rational development of drugs acting at this important group of targets.

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