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Cited by 72Receptor Mechanisms and SignalingNeuroendocrine regulation and behaviorNeuropeptides and Animal Physiology

The Proximal Portion of the COOH Terminus of the Oxytocin Receptor Is Required for Coupling to Gq, but Not Gi

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Hoare, Sarasija, Copland, John A., Strakova, Zuzana, Ives, Kirk, Jeng, Yow-Jiun, Hellmich, Mark R., Soloff, Melvyn S.·1999·Journal of Biological Chemistry
DOI 10.1074/jbc.274.40.28682
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Abstract

As the oxytocin receptor plays a key role in parturition and lactation, there is considerable interest in defining its structure/functional relationships. We previously showed that the rat oxytocin receptor transfected into Chinese hamster ovary cells was coupled to both G(q/11) and G(i/o), and that oxytocin stimulated ERK-2 phosphorylation and prostaglandin E(2) synthesis via protein kinase C activity. In this study, we show that deletion of 51 amino acid residues from the carboxyl terminus resulted in reduced affinity for oxytocin and a corresponding rightward shift in the dose-response curve for oxytocin-stimulated [Ca(2+)](i). However, oxytocin-stimulated ERK-2 phosphorylation and prostaglandin E(2) synthesis did not occur in cells expressing the truncated receptor. Oxytocin also failed to increase phospholipase A activity or activate protein kinase C, indicating that the mutant receptor is uncoupled from G(q)-mediated pathways. The Delta51 receptor is coupled to G(i), as oxytocin-stimulated Ca(2+) transients were inhibited by pertussis toxin, and a Gbetagamma sequestrant. Preincubation of Delta51 cells with the tyrosine kinase inhibitor, genistein, also blocked the oxytocin effect. A Delta39 mutant had all the activities of the wild type oxytocin receptor. These results show that the portion between 39 and 51 residues from the COOH terminus of the rat oxytocin receptor is required for interaction with G(q/11), but not G(i/o). Furthermore, an increase in intracellular calcium was generated via a G(i)betagamma-tyrosine kinase pathway from intracellular stores that are distinct from G(q)-mediated inositol trisphosphate-regulated stores.

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Crossref · 10.1074/jbc.274.40.28682

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  • Experimental truncation of the C-terminus before the palmitoylation site results in reductions in receptor expression, binding affinity, and Ca2+ response, and an overall shift from Gq to Gi coupling.

    “Experimental truncation of the C-terminus before the palmitoylation site results in reductions in receptor expression, binding affinity, and Ca2+ response, and an overall shift from Gq to Gi coupling (Hoare et al., 1999).”

    From Neuropeptide diversity and the regulation of social behavior in New World primates (2016) · cites this paper as Hoare et al., 1999

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Authors
Hoare, S., Copland, J. A., Strakova, Z., Ives, K., Jeng, Y.-J., Hellmich, M. R., & Soloff, M. S.
Affiliations
The University of Texas Medical Branch at Galveston (US)
Corresponding author
Soloff, Melvyn S.
ORCID
Copland, John A.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1999-10
Volume
274
Issue
40
Pages
28682-28689
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.274.40.28682
OpenAlex
W1987672555
Cited by
72
References
65
Citations by year
2025: 1 · 2023: 1 · 2022: 3 · 2021: 2 · 2020: 3 · 2019: 1 · 2018: 2 · 2017: 1 · 2016: 1 · 2014: 2 · 2013: 7
FWCI
2.19
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
  • National Institutes of Health (5r01hd026168-10)
  • Eunice Kennedy Shriver National Institute of Child Health and Human Development (HD26168)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Receptor Mechanisms and Signaling
  • Social Sciences › Psychology › Social Psychology › Neuroendocrine regulation and behavior
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuropeptides and Animal Physiology
Keywords
oxytocin receptor, carboxyl terminus, Gq/11 coupling, G protein coupling, intracellular calcium, prostaglandin E2 synthesis, protein kinase C, pertussis toxin, tyrosine kinase, genistein
MeSH terms
Amino Acid Sequence, Animals, Calcium, Cricetinae, Humans, Inositol Phosphates, Molecular Sequence Data, Oxytocin, Phosphorylation, Mutagenesis, CHO Cells, Sequence Deletion, Sequence Homology, Amino Acid, Receptors, Oxytocin, GTP-Binding Proteins, Mitogen-Activated Protein Kinase 1, Mitogen-Activated Protein Kinases, p38 Mitogen-Activated Protein Kinases

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