Signaling involved in PTTH-stimulated 4E-BP phosphorylation in prothoracic gland cells of Bombyx mori

Gu, Shi‐Hong; Hsieh, Yun-Chih; Lin, Pei‐Ling

doi:10.1016/j.jinsphys.2016.10.007

Cited by 9 publications

(6 citation statements)

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“…In addition, when PGs were treated with extracellular fluid from cells only or cells infected with WT AcMNPV, no activation of JNK phosphorylation was observed (O'Reilly et al, 1995 ); this indicates the specificity of the recombinant PTTH (Figure 2D ). Treatment with the PTTH, but not with extracellular fluid from cells only or cells infected with the WT AcMNPV, stimulated ERK and 4E-BP phosphorylation, two well-documented signaling pathways downstream of PTTH stimulation (Gu et al, 2010 , 2017 ), further confirming the specificity of the recombinant PTTH in the present study.…”

Section: Resultssupporting

confidence: 87%

“…The pathways that mediate ecdysteroidogenesis in response to PTTH stimulation are complex and not fully understood at the molecular level. Several studies demonstrated the involvement of the PKA, PKC, ERK, and AMPK/TOR signaling pathways (Smith and Rybczynski, 2012 ; Gu et al, 2017 ). In the present study, we demonstrated that PTTH stimulates phosphorylation of JNK in B. mori PGs.…”

Section: Discussionmentioning

confidence: 99%

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Stimulation of JNK Phosphorylation by the PTTH in Prothoracic Glands of the Silkworm, Bombyx mori

Hsieh

et al. 2018

Front. Physiol.

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In this study, phosphorylation of c-Jun N-terminal kinase (JNK) by the prothoracicotropic hormone (PTTH) was investigated in prothoracic glands (PGs) of the silkworm, Bombyx mori. Results showed that JNK phosphorylation was stimulated by the PTTH in time- and dose-dependent manners. In vitro activation of JNK phosphorylation in PGs by the PTTH was also confirmed in an in vivo experiment, in which a PTTH injection greatly increased JNK phosphorylation in PGs of day-6 last instar larvae. JNK phosphorylation caused by PTTH stimulation was greatly inhibited by U73122, a potent and specific inhibitor of phospholipase C (PLC) and an increase in JNK phosphorylation was also detected when PGs were treated with agents (either A23187 or thapsigargin) that directly elevated the intracellular Ca2+ concentration, thereby indicating involvement of PLC and Ca2+. Pretreatment with an inhibitor (U0126) of mitogen-activated protein kinase (MAPK)/extracellular signal-regulated kinase (ERK) kinase (MEK) and an inhibitor (LY294002) of phosphoinositide 3-kinase (PI3K) failed to significantly inhibit PTTH-stimulated JNK phosphorylation, indicating that ERK and PI3K were not related to JNK. We further investigated the effect of modulation of the redox state on JNK phosphorylation. In the presence of either an antioxidant (N-acetylcysteine, NAC) or diphenylene iodonium (DPI), PTTH-stimulated JNK phosphorylation was blocked. The JNK kinase inhibitor, SP600125, markedly inhibited PTTH-stimulated JNK phosphorylation and ecdysteroid synthesis. The kinase assay of JNK in PGs confirmed its stimulation by PTTH and inhibition by SP600125. Moreover, PTTH treatment did not affect JNK or Jun mRNA expressions. Based on these findings, we concluded that PTTH stimulates JNK phosphorylation in Ca2+- and PLC-dependent manners and that the redox-regulated JNK signaling pathway is involved in PTTH-stimulated ecdysteroid synthesis in B. mori PGs.

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Section: Resultssupporting

confidence: 87%

Section: Discussionmentioning

confidence: 99%

Stimulation of JNK Phosphorylation by the PTTH in Prothoracic Glands of the Silkworm, Bombyx mori

Hsieh

et al. 2018

Front. Physiol.

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“…Cotesia flavipes parasitization of D. saccharalis larvae led to the down-regulation of enzymes acting on ecdysteroid synthesis and of several eukaryotic translation initiation factors. Eukaryotic translation initiation factors also participate in regulating the activity of prothoracic glands as signaling factors (Gu et al, 2017). Down-regulation of ecdysteroid synthesis was followed by the negative regulation of many orphan nuclear receptors, such as the nuclear hormone receptors HR3, E75 and E74.…”

Section: Discussionmentioning

confidence: 99%

Regulation of the Larval Transcriptome of Diatraea saccharalis (Lepidoptera: Crambidae) by Maternal and Other Factors of the Parasitoid Cotesia flavipes (Hymenoptera: Braconidae)

Merlin

Cônsoli

2019

Front. Physiol.

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Koinobiont endoparasitoid wasps regulate the host’s physiology to their own benefit during their growth and development, using maternal, immature and/or derived-tissue weaponry. The tools used to subdue the wasps’ hosts interfere directly with host transcription activity. The broad range of host tissues and pathways affected impedes our overall understanding of the host-regulation process during parasitoid development. Next-generation sequencing and de novo transcriptomes are helpful approaches to broad questions, including in non-model organisms. In the present study, we used Illumina sequencing to assemble a de novo reference transcriptome of the sugarcane borer Diatraea saccharalis, to investigate the regulation of host gene expression by the larval endoparasitoid Cotesia flavipes. We obtained 174,809,358 reads and assembled 144,116 transcripts, of which 44,325 were putatively identified as lepidopteran genes and represented a substantial number of pathways that are well described in other lepidopteran species. Comparative transcriptome analyses of unparasitized versus parasitized larvae identified 1,432 transcripts of D. saccharalis that were up-regulated under parasitization by C. flavipes, while 1,027 transcripts were down-regulated. Comparison of the transcriptomes of unparasitized and pseudoparasitized D. saccharalis larvae led to the identification of 1,253 up-regulated transcripts and 972 down-regulated transcripts in the pseudoparasitized larvae. Analysis of the differentially expressed transcripts showed that C. flavipes regulated several pathways, including the Ca+2 transduction signaling pathway, glycolysis/gluconeogenesis, chitin metabolism, and hormone biosynthesis and degradation, as well as the immune system, allowing us to identify key target genes involved in the metabolism and development of D. saccharalis.

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“…Their respective recombinant IAGs increase MAPK/ERK phosphorylation in M. rosenbergii , S. verreauxi , and Cherax quadricarinatus testis explants in vitro ( 124 ). In insects, ILPs (e.g., Dilps1-6 in D. melanogaster and Bombyxin in Bombyx mori ) stimulate PI3K/Akt signaling and mTORC1-dependent ecdysteroidogenesis in the insect PG ( 78 , 97 , 106 , 107 , 126 – 129 ). Based on these data, a model for ILP signaling in the YO is proposed ( Figure 4 ).…”

Section: Receptor Tyrosine Kinasesmentioning

confidence: 99%

Signaling Pathways That Regulate the Crustacean Molting Gland

Mykles

2021

Front. Endocrinol.

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A pair of Y-organs (YOs) are the molting glands of decapod crustaceans. They synthesize and secrete steroid molting hormones (ecdysteroids) and their activity is controlled by external and internal signals. The YO transitions through four physiological states over the molt cycle, which are mediated by molt-inhibiting hormone (MIH; basal state), mechanistic Target of Rapamycin Complex 1 (mTORC1; activated state), Transforming Growth Factor-β (TGFβ)/Activin (committed state), and ecdysteroid (repressed state) signaling pathways. MIH, produced in the eyestalk X-organ/sinus gland complex, inhibits the synthesis of ecdysteroids. A model for MIH signaling is organized into a cAMP/Ca2+-dependent triggering phase and a nitric oxide/cGMP-dependent summation phase, which maintains the YO in the basal state during intermolt. A reduction in MIH release triggers YO activation, which requires mTORC1-dependent protein synthesis, followed by mTORC1-dependent gene expression. TGFβ/Activin signaling is required for YO commitment in mid-premolt. The YO transcriptome has 878 unique contigs assigned to 23 KEGG signaling pathways, 478 of which are differentially expressed over the molt cycle. Ninety-nine contigs encode G protein-coupled receptors (GPCRs), 65 of which bind a variety of neuropeptides and biogenic amines. Among these are putative receptors for MIH/crustacean hyperglycemic hormone neuropeptides, corazonin, relaxin, serotonin, octopamine, dopamine, allatostatins, Bursicon, ecdysis-triggering hormone (ETH), CCHamide, FMRFamide, and proctolin. Contigs encoding receptor tyrosine kinase insulin-like receptor, epidermal growth factor (EGF) receptor, and fibroblast growth factor (FGF) receptor and ligands EGF and FGF suggest that the YO is positively regulated by insulin-like peptides and growth factors. Future research should focus on the interactions of signaling pathways that integrate physiological status with environmental cues for molt control.

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Signaling involved in PTTH-stimulated 4E-BP phosphorylation in prothoracic gland cells of Bombyx mori

Cited by 9 publications

References 50 publications

Stimulation of JNK Phosphorylation by the PTTH in Prothoracic Glands of the Silkworm, Bombyx mori

Stimulation of JNK Phosphorylation by the PTTH in Prothoracic Glands of the Silkworm, Bombyx mori

Regulation of the Larval Transcriptome of Diatraea saccharalis (Lepidoptera: Crambidae) by Maternal and Other Factors of the Parasitoid Cotesia flavipes (Hymenoptera: Braconidae)

Signaling Pathways That Regulate the Crustacean Molting Gland

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