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| Natura: | Artículo científico |
| Lingua: | en |
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The Journal of experimental biology
2025
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| Accesso online: | https://pubmed.ncbi.nlm.nih.gov/39850985/ |
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| author | Head, Talia B Pérez-Moreno, Jorge L Ventura, Tomer Durica, David S Mykles, Donald L |
| author_facet | Head, Talia B Pérez-Moreno, Jorge L Ventura, Tomer Durica, David S Mykles, Donald L Head, Talia B Pérez-Moreno, Jorge L Ventura, Tomer Durica, David S Mykles, Donald L |
| collection | PubMed - marine biology |
| contents | Two cGMP-dependent protein kinases have opposing effects on molt-inhibiting hormone regulation of Y-organ ecdysteroidogenesis. Head, Talia B Pérez-Moreno, Jorge L Ventura, Tomer Durica, David S Mykles, Donald L Animals Ecdysteroids Cyclic GMP-Dependent Protein Kinases Invertebrate Hormones Brachyura Phylogeny Molting Arthropod Proteins Decapod crustaceans regulate molting through steroid molting hormones (ecdysteroids) synthesized by the molting gland (Y-organ, YO). Molt-inhibiting hormone (MIH), a neuropeptide synthesized and secreted by the eyestalk ganglia, negatively regulates YO ecdysteroidogenesis. MIH signaling is mediated by cyclic nucleotide second messengers. cGMP-dependent protein kinase (PKG) is the presumed effector of MIH signaling by inhibiting mechanistic Target of Rapamycin Complex 1 (mTORC1)-dependent ecdysteroidogenesis. Phylogenetic analysis of PKG contiguous sequences in CrusTome, as well as 35 additional species in NCBI RefSeq, identified 206 PKG1 sequences in 108 species and 59 PKG2 sequences in 53 species. These included four PKG1α splice variants in the N-terminal region that were unique to decapods, as well as PKG1β and PKG2 homologs. In vitro assays using YOs from the blackback land crab (Gecarcinus lateralis) and green shore crab (Carcinus maenas) determined the effects of MIH±PKG inhibitors on ecdysteroid secretion. A general PKG inhibitor, Rp-8-Br-PET-cGMPS, countered the effects of MIH, as ecdysteroid secretion increased in PKG-inhibited YOs compared with C. maenas YOs incubated with MIH alone. By contrast, a PKG2-specific inhibitor, AP-C5 {4-(4-[1H-imidazol-1-yl]phenyl)-N-2-propyn-1-yl-2-pyrimidinamine}, enhanced the effects of MIH, as ecdysteroid secretion decreased in G. lateralis and C. maenas YOs incubated with AP-C5 and MIH compared with YOs incubated with MIH alone. These data suggest that both PKG1 and PKG2 are activated by MIH, but have opposing effects on mTORC1-dependent ecdysteroidogenesis. A model is proposed in which the dominant role of PKG1 is countered by PKG2, resulting in low ecdysteroid production by the basal YO during intermolt. |
| format | Artículo científico |
| id | pubmed_39850985 |
| institution | PubMed |
| language | en |
| publishDate | 2025 |
| publisher | The Journal of experimental biology |
| record_format | pubmed |
| spellingShingle | Two cGMP-dependent protein kinases have opposing effects on molt-inhibiting hormone regulation of Y-organ ecdysteroidogenesis. Head, Talia B Pérez-Moreno, Jorge L Ventura, Tomer Durica, David S Mykles, Donald L Animals Ecdysteroids Cyclic GMP-Dependent Protein Kinases Invertebrate Hormones Brachyura Phylogeny Molting Arthropod Proteins Two cGMP-dependent protein kinases have opposing effects on molt-inhibiting hormone regulation of Y-organ ecdysteroidogenesis. Head, Talia B Pérez-Moreno, Jorge L Ventura, Tomer Durica, David S Mykles, Donald L Animals Ecdysteroids Cyclic GMP-Dependent Protein Kinases Invertebrate Hormones Brachyura Phylogeny Molting Arthropod Proteins Decapod crustaceans regulate molting through steroid molting hormones (ecdysteroids) synthesized by the molting gland (Y-organ, YO). Molt-inhibiting hormone (MIH), a neuropeptide synthesized and secreted by the eyestalk ganglia, negatively regulates YO ecdysteroidogenesis. MIH signaling is mediated by cyclic nucleotide second messengers. cGMP-dependent protein kinase (PKG) is the presumed effector of MIH signaling by inhibiting mechanistic Target of Rapamycin Complex 1 (mTORC1)-dependent ecdysteroidogenesis. Phylogenetic analysis of PKG contiguous sequences in CrusTome, as well as 35 additional species in NCBI RefSeq, identified 206 PKG1 sequences in 108 species and 59 PKG2 sequences in 53 species. These included four PKG1α splice variants in the N-terminal region that were unique to decapods, as well as PKG1β and PKG2 homologs. In vitro assays using YOs from the blackback land crab (Gecarcinus lateralis) and green shore crab (Carcinus maenas) determined the effects of MIH±PKG inhibitors on ecdysteroid secretion. A general PKG inhibitor, Rp-8-Br-PET-cGMPS, countered the effects of MIH, as ecdysteroid secretion increased in PKG-inhibited YOs compared with C. maenas YOs incubated with MIH alone. By contrast, a PKG2-specific inhibitor, AP-C5 {4-(4-[1H-imidazol-1-yl]phenyl)-N-2-propyn-1-yl-2-pyrimidinamine}, enhanced the effects of MIH, as ecdysteroid secretion decreased in G. lateralis and C. maenas YOs incubated with AP-C5 and MIH compared with YOs incubated with MIH alone. These data suggest that both PKG1 and PKG2 are activated by MIH, but have opposing effects on mTORC1-dependent ecdysteroidogenesis. A model is proposed in which the dominant role of PKG1 is countered by PKG2, resulting in low ecdysteroid production by the basal YO during intermolt. |
| title | Two cGMP-dependent protein kinases have opposing effects on molt-inhibiting hormone regulation of Y-organ ecdysteroidogenesis. |
| topic | Animals Ecdysteroids Cyclic GMP-Dependent Protein Kinases Invertebrate Hormones Brachyura Phylogeny Molting Arthropod Proteins |
| url | https://pubmed.ncbi.nlm.nih.gov/39850985/ |