Identification and signaling characterization of four urotensin II receptor subtypes in the western clawed frog, Xenopus tropicalis
•Four functional UTR (UTR1, UTR3, UTR4, and UTR5) subtypes are present in X. tropicalis.•UTR1 and UTR5 are most likely linked to PLC/PKC and GEF-H1/RhoA/ROCK/MLC signaling.•UTR3 and UTR4 are likely linked to GEF-H1/RhoA/ROCK/MLC signaling via the G12/13 protein.•Similarity between Xenopus UTR1 and U...
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Published in | General and comparative endocrinology Vol. 299; p. 113586 |
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Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
Elsevier Inc
01.12.2020
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Subjects | |
Online Access | Get full text |
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Summary: | •Four functional UTR (UTR1, UTR3, UTR4, and UTR5) subtypes are present in X. tropicalis.•UTR1 and UTR5 are most likely linked to PLC/PKC and GEF-H1/RhoA/ROCK/MLC signaling.•UTR3 and UTR4 are likely linked to GEF-H1/RhoA/ROCK/MLC signaling via the G12/13 protein.•Similarity between Xenopus UTR1 and UTR5 suggests that local duplication might have occurred.
Urotensin II (UII) is involved, via the UII receptor (UTR), in many physiological and pathological processes, including vasoconstriction, locomotion, osmoregulation, immune response, and metabolic syndrome. In silico studies have revealed the presence of four or five distinct UTR (UTR1–UTR5) gene sequences in nonmammalian vertebrates. However, the functionality of these receptor subtypes and their associations to signaling pathways are unclear. In this study, full-length cDNAs encoding four distinct UTR subtypes (UTR1, UTR3, UTR4, and UTR5) were isolated from the western clawed frog (Xenopus tropicalis). In functional analyses, homologous Xenopus UII stimulation of cells expressing UTR1 or UTR5 induced intracellular calcoum mobilization and phosphorylation of extracellular signal-regulated kinase 1/2. Cells expressing UTR3 or UTR4 did not show this response. Furthermore, UII induced the phosphorylation of cyclic adenosine monophosphate (cAMP) response element binding protein (CREB) through the UII–UTR1/5 system. However, intracellular cAMP accumulation was not observed, suggesting that UII-induced CREB phosphorylation is caused by a signaling pathway different from that involving Gs protein. In contrast, the administration of UII to cells increased the phosphorylation of guanine nucleotide exchange factor-H1 (GEF-H1) and myosin light chain 2 (MLC2) in all UTR subtypes. These results define four distinct UTR functional subtypes and are consistent with the molecular evolution of UTR subtypes in vertebrates. Further understanding of signaling properties associated with UTR subtypes may help in clarifying the functional roles associated with UII–UTR interactions in nonmammalian vertebrates. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0016-6480 1095-6840 |
DOI: | 10.1016/j.ygcen.2020.113586 |