Identification of Amino Acid Residues That Direct Differential Ligand Selectivity of Mammalian and Nonmammalian V1a Type Receptors for Arginine Vasopressin and Vasotocin

Acharjee, Sujata; Do-Rego, Jean Luc; Oh, Da Young; Ahn, Ryun Sup; Choe, Han; Vaudry, Hubert; Kim, Kyungjin; Seong, Jae Young; Kwon, Ho

doi:10.1074/jbc.m408909200

Cited by 39 publications

(35 citation statements)

References 48 publications

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“…Evolutionary pressure preserves the amino acid residues that are essential for the basic protein structure and for primary interactions between ligand and receptor family members. Specific changes in the amino acid sequence permit selective interaction between a ligand-receptor pair (53)(54)(55)(56)(57). In the former case, residues are conserved across paralogous members.…”

Section: Discussionmentioning

confidence: 99%

Ligand Binding Pocket Formed by Evolutionarily Conserved Residues in the Glucagon-like Peptide-1 (GLP-1) Receptor Core Domain

Moon

Lee

Park

et al. 2015

Journal of Biological Chemistry

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Background:Little is known about the interaction between GLP-1 and the heptahelical core domain of GLP1R. Results: GLP-1 Asp 9 and Gly 4 interact with the evolutionarily conserved residues in extracellular loop 3. Conclusion: Ligand binding pocket formed by evolutionarily conserved residues in the GLP1R core domain. Significance: This study highlights the mechanism underlying high affinity interaction between GLP-1 and the binding pocket of the receptor.

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Section: Discussionmentioning

confidence: 99%

Ligand Binding Pocket Formed by Evolutionarily Conserved Residues in the Glucagon-like Peptide-1 (GLP-1) Receptor Core Domain

Moon

Lee

Park

et al. 2015

Journal of Biological Chemistry

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“…The VT1 receptor is most similar to the mammalian V 1a receptor. Although its sequence identity with the mammalian V 1a is not particularly high (51.9% with the rat V 1a ; Tan et al, 2000), the avian VT1 receptor contains amino acid residues that are important for the ligand selectivity of the mammalian V 1a receptor, and the pharmacology of the avian VT1 is therefore more similar to the mammalian V 1a than are V 1a -like receptors in other non-mammalian taxa (see functional studies in Acharjee et al, 2004). Thus, we here used an iodinated, linear V 1a antagonist (Phenylacetyl 1 , 0-Me-D-Tyr 2 , [ 125 I-Arg 6 ]-) (Perkin-Elmer) that has a very high affinity for mammalian V 1a receptors, and a much more modest affinity for V 1b receptors (Barberis et al, 1995;Young et al, 1997).…”

Section: Nih-pa Author Manuscriptmentioning

confidence: 99%

Neuropeptide binding reflects convergent and divergent evolution in species-typical group sizes

Goodson

Evans

Wang

2006

Hormones and Behavior

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Neuroendocrine factors that produce species differences in aggregation behavior ("sociality") are largely unknown, although relevant studies should yield important insights into mechanisms of affiliation and social evolution. We here focused on five species in the avian family Estrildidae that differ selectively in their species-typical group sizes (all species are monogamous and occupy similar habitats). These include two highly gregarious species that independently evolved coloniality; two territorial species that independently evolved territoriality; and an intermediate, modestly gregarious species that is a sympatric congener of one of the territorial species. Using males and females of each species, we examined binding sites for 125 I-vasoactive intestinal polypeptide (VIP), 125 I-sauvagine (SG; a ligand for corticotropin releasing factor, CRF, receptors) and a linear 125 I-V 1a vasopressin antagonist (to localize receptors for vasotocin, VT). VIP, CRF and VT are neuropeptides that influence stress, anxiety and/or various social behaviors. For numerous areas (particularly within the septal complex), binding densities in the territorial species differed significantly from binding in the more gregarious species, and in most of these cases, binding densities for the moderately greagarious species were either comparable to the two colonial species, or were intermediate to the territorial and colonial species. Such patterns were observed for 125 I-VIP binding in the medial bed nucleus of the stria terminalis, medial septum, septohippocampal septum, and subpallial zones of the lateral septum; for 125 I-SG binding in the infundibular hypothalamus, and lateral and medial divisions of the ventromedial hypothalamus; and for the linear 125 I-V 1a antagonist in the medial septum, and the pallial and subpallial zones of the caudal lateral septum. With the exception of 125 I-SG binding in the infundibular hypothalamus, binding densitites are positively related to sociality. Keywords lateral septum; hypothalamus; vasotocin; vasopressin; corticotropin releasing factor; vasoactive intestinal polypeptide; evolution; sociality; songbird Components of social organization can change rapidly during evolution, as suggested by the fact that many vertebrate groups exhibit substantial diversity in behavioral dimensions such as grouping, mating systems, patterns of parental care, philopatry and kin affiliation. Thus, a given form of behavior or social structure may have evolved independently many times in various vertebrate lineages. Somewhat inconveniently, the evolution of a given species-typical social structure could hypothetically be produced by more than one kind of evolutionary modification to the brain, reducing our ability to generalize across species. Species-typical group size ("sociality") provides a good example: Natural selection on aggregation behavior could conceivably act on neural mechanisms that relate to anxiety, stress, aggression, reward, bonding, and/or simple arousal to social stimuli 1 . Therefore, in...

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“…Site-directed mutagenesis of human GPR92 was generated by the PCR overlapping extension method (11). All PCR-derived sequences were verified by automatic sequencing.…”

Section: Methodsmentioning

confidence: 99%

Identification of Farnesyl Pyrophosphate and N-Arachidonylglycine as Endogenous Ligands for GPR92

Yoon

Moon

et al. 2008

Journal of Biological Chemistry

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A series of small compounds acting at the orphan G proteincoupled receptor GPR92 were screened using a signaling pathway-specific reporter assay system. Lipid-derived molecules including farnesyl pyrophosphate (FPP), N-arachidonylglycine (NAG), and lysophosphatidic acid were found to activate GPR92. FPP and lysophosphatidic acid were able to activate both G q/11 -and G s -mediated signaling pathways, whereas NAG activated only the G q/11 -mediated signaling pathway. Computer-simulated modeling combined with site-directed mutagenesis of GPR92 indicated that Thr 97 , Gly 98 , Phe 101 , and Arg 267 of GPR92 are responsible for the interaction of GPR92 with FPP and NAG. Reverse transcription-PCR analysis revealed that GPR92 mRNA is highly expressed in the dorsal root ganglia (DRG) but faint in other brain regions. Peripheral tissues including, spleen, stomach, small intestine, and kidney also expressed GPR92 mRNA. Immunohistochemical analysis revealed that GPR92 is largely co-localized with TRPV1, a nonspecific cation channel that responds to noxious heat, in mouse and human DRG. FPP and NAG increased intracellular Ca 2؉ levels in cultured DRG neurons. These results suggest that FPP and NAG play a role in the sensory nervous system through activation of GPR92.

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Identification of Amino Acid Residues That Direct Differential Ligand Selectivity of Mammalian and Nonmammalian V1a Type Receptors for Arginine Vasopressin and Vasotocin

Cited by 39 publications

References 48 publications

Ligand Binding Pocket Formed by Evolutionarily Conserved Residues in the Glucagon-like Peptide-1 (GLP-1) Receptor Core Domain

Ligand Binding Pocket Formed by Evolutionarily Conserved Residues in the Glucagon-like Peptide-1 (GLP-1) Receptor Core Domain

Neuropeptide binding reflects convergent and divergent evolution in species-typical group sizes

Identification of Farnesyl Pyrophosphate and N-Arachidonylglycine as Endogenous Ligands for GPR92

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