Structure of the Third Intracellular Loop of the Vasopressin V2 Receptor and Conformational Changes upon Binding to gC1qR

Bellot, Gaëtan; Granier, Sébastien; Bourguet, William; Seyer, René; Rahmeh, Rita; Mouillac, Bernard; Pascal, Robert; Mendre, Christiane; Déméné, Hélène

doi:10.1016/j.jmb.2009.02.065

Cited by 16 publications

(12 citation statements)

References 87 publications

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“…The expansion of ICL III seems to be a teleost-specific event (Ocampo Daza et al 2012). The ICL III may be critical for receptor signal transduction, as reported in the mammalian V2 type receptor (Liu and Wess 1996;Bellot et al 2009;Erlenbach and Wess 1998). In the catfish, the V2R ICL III has 22 Lys/ Arg residues while it is just the half in V1a1R and V1a2R.…”

Section: Structural Characteristics Of the Putative Vt Receptorsmentioning

confidence: 88%

Molecular cloning, sequencing and phylogeny of vasotocin receptor genes in the air-breathing catfish Heteropneustes fossilis with sex dimorphic and seasonal variations in tissue expression

Rawat

Chaube

Joy

2015

Fish Physiol Biochem

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Vasotocin (VT) is the ortholog of vasopressin (VP) in non-mammalian vertebrates and is known for multiple functions. Teleost fishes have a complete repertoire of known VP/VT receptor subtypes (vasopressin type, VR): two V1A subtypes (V1Aa and V1Ab or V1a1 and V1a2) and five V2 subtypes (V2A1, V1A2, V2B1, V2B2 and V2C). Full-length cDNAs of v1a1, v1a2 and v2 (v2a1) with ORFs of 1,308, 1,137 and 1,527 bp, respectively, were cloned and characterized in the catfish Heteropneustes fossilis (Siluriformes, Ostariophysi). BLAST analysis revealed that the genes encoded three VT receptors, V1a1, V1a2 and V2 of 436, 379 and 509 amino acid residues, respectively. The predicted proteins showed typical features of the seven-transmembrane domain receptor core structure with hallmark triplets Asp-Arg-Tyr/Asp-Arg-His (DRY/DRH) and the variable intracellular loop III of vertebrate neurohypophysial hormone receptors. Phylogenetic analysis of the deduced protein sequences revealed that they clustered with the V1Aa, V1Ab and V2A1, respectively, of other teleosts. The V2R has a sequence identity of 70-76% with V2A1 than with the V2B type (sequence identity 43-49%). Semiquantitative PCR analysis showed that the receptor gene transcripts were expressed ubiquitously in the tissues examined (brain, pituitary, gonads, liver, muscle, kidney and gills) and displayed sex and seasonal fluctuations in a tissue-specific manner. The results form a basis for functional studies on the VT receptors in the catfish.

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Section: Structural Characteristics Of the Putative Vt Receptorsmentioning

confidence: 88%

Molecular cloning, sequencing and phylogeny of vasotocin receptor genes in the air-breathing catfish Heteropneustes fossilis with sex dimorphic and seasonal variations in tissue expression

Rawat

Chaube

Joy

2015

Fish Physiol Biochem

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“…It is suggested that the receptor sites near the mem brane responsible for interaction with G proteins in most cases are in the helical conformation, which is the most optimal for interaction with the G protein α subunit (Okuda et al, 2002;Kikkou et al, 2008;Wu et al, 2008;Bellot et al, 2009). In spite of many of these sites containing a significant number of AAR destabilizing helices, some of them indeed have the ability to form helical structures.…”

Section: Discussionmentioning

confidence: 99%

“…In spite of many of these sites containing a significant number of AAR destabilizing helices, some of them indeed have the ability to form helical structures. Stabilization of these structures is realized by their neighbor helical trans membrane domains, as well as due to their interaction with the receptor complementary sites and the hydro phobic membrane phase (Okuda et al, 2002;Naider et al, 2005;Kikkou et al, 2008;Wu et al, 2008;Bellot et al, 2009). Based on this, it was suggested that the helical conformation was necessary for realization by peptides derived from the receptor CL of biological activity, which should be taken into account during the search for and construction of such peptides (Okuda et al, 2002;Naider et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

“…Many of the peptides derived from the CL 3 N and C terminal regions form helical structures in the presence of trif luoroethanol (TFE) stabilizing the helical conforma tion of peptides as well as of compounds imitating the membrane surface, such as dodecylphosphocholine (Okuda et al, 2002;Kikkou et al, 2008;Wu et al, 2008;Bellot et al, 2009). This agrees with results of theoretical and crystallographical studies of the sec ondary structure of serpentine type receptors, which indicate that the N and C terminal CL 3 regions involved in interaction with G proteins are able in many receptors to form helices that are a cytoplasmic continuation of highly spiralized transmembrane domains (Naider et al, 2005).…”

Section: The Secondary Structure Of Peptides Derived From the Third Imentioning

confidence: 99%

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The secondary structure of peptides derived from the third intracellular loop of the serpentine-type receptors and its interrelation with their biological activity

et al. 2012

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“…It seems that the important residues are dispersed widely at different positions with no common motif. This is probably because the 2nd and 3rd intracellular loops and the COOH terminal are organized together in a three-dimensional structure that binds the G protein (3,17). By interfering with the coupling of the G protein, the Ser329Arg substitution could potentially cause inhibition of the intracellular receptor signaling, resulting in a diminished production of cAMP upon stimulation.…”

Section: Discussionmentioning

confidence: 99%

Diverse vasopressin V2 receptor functionality underlying partial congenital nephrogenic diabetes insipidus

Faerch

Christensen

Rittig

et al. 2009

American Journal of Physiology-Renal Physiology

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X-linked congenital nephrogenic diabetes insipidus (CNDI) is characterized by a defective renal response to the antidiuretic hormone (AVP) due to variations in the arginine vasopressin receptor 2 ( AVPR2) gene. In a unique group of patients, the renal insensitivity to the effects of AVP is incomplete resulting in a partial phenotype. To investigate the molecular defects, two previously published variations in the AVPR2 gene, known to cause a partial CNDI phenotype, were expressed in transiently transfected human embryonic kidney cells. One variation (p.Arg104Cys) is located in the first extracellular loop and the other variation (p.Ser329Arg) is located in the intracellular COOH terminal of the receptor protein. Western blotting showed almost equal amounts of WT-V2R and Arg104Cys-V2R protein at steady state, whereas the level of Ser329Arg-V2R protein was lower. Confocal microscopy established that WT-V2R and Arg104Cys-V2R are localized on the cellular surface while the Ser329Arg-V2R primarily accumulates within the endoplasmic reticulum resulting in reduced surface expression. Ligand binding analysis demonstrated that the Bmax for cells expressing Arg104Cys-V2R and Ser329Arg-V2R were 14.8- and 2.5-fold lower than Bmax for WT-V2R, respectively. AVP affinity (1/ Kd) for WT-V2R and the Ser329Arg-V2R was similar while 1/ Kd for Arg104Cys-V2R was increased. cAMP assay revealed that cells expressing p.Arg104Cys-V2R or p.Ser329Arg-V2R produced 1.7- and 6.8-fold lower amounts of cAMP compared with WT-V2R, respectively. In conclusion, ligand binding and signal transduction capability are dependent on localization of the amino acid variation. Striking divergences at the level of receptor functionality may thus underlie similar clinical phenotypes in CNDI.

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Structure of the Third Intracellular Loop of the Vasopressin V2 Receptor and Conformational Changes upon Binding to gC1qR

Cited by 16 publications

References 87 publications

Molecular cloning, sequencing and phylogeny of vasotocin receptor genes in the air-breathing catfish Heteropneustes fossilis with sex dimorphic and seasonal variations in tissue expression

Molecular cloning, sequencing and phylogeny of vasotocin receptor genes in the air-breathing catfish Heteropneustes fossilis with sex dimorphic and seasonal variations in tissue expression

The secondary structure of peptides derived from the third intracellular loop of the serpentine-type receptors and its interrelation with their biological activity

Diverse vasopressin V2 receptor functionality underlying partial congenital nephrogenic diabetes insipidus

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