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Int J Mol Sci
2020 Nov 12;2122:. doi: 10.3390/ijms21228544.
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Invertebrate Gonadotropin-Releasing Hormone Receptor Signaling and Its Relevant Biological Actions.
Sakai T
,
Yamamoto T
,
Matsubara S
,
Kawada T
,
Satake H
.
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Gonadotropin-releasing hormones (GnRHs) play pivotal roles in reproduction via the hypothalamus-pituitary-gonad axis (HPG axis) in vertebrates. GnRHs and their receptors (GnRHRs) are also conserved in invertebrates lacking the HPG axis, indicating that invertebrate GnRHs do not serve as "gonadotropin-releasing factors" but, rather, function as neuropeptides that directly regulate target tissues. All vertebrate and urochordate GnRHs comprise 10 amino acids, whereas amphioxus, echinoderm, and protostome GnRH-like peptides are 11- or 12-residue peptides. Intracellular calcium mobilization is the major second messenger for GnRH signaling in cephalochordates, echinoderms, and protostomes, while urochordate GnRHRs also stimulate cAMP production pathways. Moreover, the ligand-specific modulation of signal transduction via heterodimerization between GnRHR paralogs indicates species-specific evolution in Ciona intestinalis. The characterization of authentic or putative invertebrate GnRHRs in various tissues and their in vitro and in vivo activities indicate that invertebrate GnRHs are responsible for the regulation of both reproductive and nonreproductive functions. In this review, we examine our current understanding of and perspectives on the primary sequences, tissue distribution of mRNA expression, signal transduction, and biological functions of invertebrate GnRHs and their receptors.
Figure 1. Signaling cascades triggered by the interaction of Ciona gonadotropin-releasing hormones (GnRHs) with the cognate receptor. (A) Interaction of tGnRH-5 with Ci-GnRHR-1 (R1) activates a calcium-independent protein kinase C (PKC), PKCζ, followed by the upregulation of extracellular signal-regulated protein kinase (ERK) phosphorylation. (B) Interaction of tGnRH-6 with R1 activates PKCζ and a calcium-dependent PKC, PKC α, leading to the upregulation of ERK phosphorylation. Both signaling pathways are potentiated via the heterodimerization of Ci-GnRHR-1 with a species-specific orphan GPCR paralog, Ci-GnRHR-4 (C,D).
Figure 2. Differential regulation of GnRH signaling pathways via GPCR heterodimerization. Heterodimerization between Ci-GnRHR-1 and -4 results in a 10-fold more potent intracellular calcium ion mobilization response to tGnRH-6 compared with the Ci-GnRHR-1 monomer/homodimer. Heterodimerization between Ci-GnRHR-2 and -4 decreases cAMP production by 50% in response to tGnRH-6, 7, and 8 compared with the Ci-GnRHR-1 monomer/homodimer.
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