G-protein αq participates in the steroid hormone 20-hydroxyecdysone nongenomic signal transduction

Ren, Jing; Li, Xiangru; Liu, Pengcheng; Cai, Mei-Juan; Liu, Wen; Wang, Jin-Xing; Zhao, Xiao‐Fan

doi:10.1016/j.jsbmb.2014.08.006

Cited by 13 publications

(10 citation statements)

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“…20E also activates the PKC pathway in B. mori (22,23) and H. armigera (18,24) and the PKA pathway in D. melanogaster (27). The PKC pathway regulates USP phosphorylation, formation of the EcR-USP transcription complex (25,26), and acetylation of USP1 (2) for 20E pathway gene expression. However, the function of the 20E-induced PKC pathway and its relationship with the 20E-induced PKA pathway are unclear.…”

Section: Discussionmentioning

confidence: 99%

“…Two ecdysone-responsive GPCRs, ErGPCR1 and ErG-PCR2, transmit the 20E signal in the cell membrane in the lepidopteran insect cotton bollworm H. armigera (18,24). The nongenomic GPCR, G␣ q , phospholipase C (PLC) ␥1, calcium, and protein kinase C (PKC) signaling cascade has been identified in H. armigera, suggesting that the activation of the PKC pathway is necessary for USP phosphorylation and 20E-responsive gene transcription in the 20E genomic pathway (25,26). 20E triggered the lysine acetylation of USP1 by activating the GPCR, PLC, Ca 2ϩ , and CaMKII signaling pathway, which is essential for the formation of the EcRB1-USP1 transcription complex and gene transcription (2).…”

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confidence: 99%

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The Steroid Hormone 20-Hydroxyecdysone Enhances Gene Transcription through the cAMP Response Element-binding Protein (CREB) Signaling Pathway

Jing

Wang

Han

et al. 2016

Journal of Biological Chemistry

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Animal steroid hormones regulate gene transcription through genomic pathways by binding to nuclear receptors. These steroid hormones also rapidly increase intracellular calcium and cyclic adenosine monophosphate (cAMP) levels and activate the protein kinase C (PKC) and protein kinase A (PKA) nongenomic pathways. However, the function and mechanism of the nongenomic pathways of the steroid hormones are unclear, and the relationship between the PKC and PKA pathways is also unclear. We propose that the steroid hormone 20-hydroxyecdysone (20E) activates the PKA pathway to enhance 20E-induced gene transcription in the lepidopteran insect Helicoverpa armigera. The expression of the catalytic subunit 1 of PKA (PKAC1) increased during metamorphosis, and PKAC1 knockdown blocked pupation and repressed

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

The Steroid Hormone 20-Hydroxyecdysone Enhances Gene Transcription through the cAMP Response Element-binding Protein (CREB) Signaling Pathway

Jing

Wang

Han

et al. 2016

Journal of Biological Chemistry

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“…The regulation of USP phosphorylation by 20E through PKC has been demonstrated in D. melanogaster (17), M. sexta (33), Tenebrio molitor (34), and H. armigera (16), although the PKC was not identified yet until now. Furthermore, EcR has been demonstrated to be a phosphoprotein in adult B. mori (18), Drosophila larvae (35), and H. armigera (19). However, these studies only demonstrated the phosphorylation of EcR and did not identify its phosphorylation sites or the specific PKC involved.…”

Section: E Up-regulates Pkcδ Expression To Promote Apoptosis Duringmentioning

confidence: 98%

“…Some unknown PKCs are involved in the phosphorylation of the heterodimeric partner USP in 20E signaling, as demonstrated by inhibitor experiments in H. armigera (16) and in Drosophila (17). EcRB1 has also been shown to be phosphorylated in Bombyx mori (18) and H. armigera (19). However, it is unknown which isoform of PKC phosphorylates EcRB1.…”

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confidence: 99%

Protein kinase C delta phosphorylates ecdysone receptor B1 to promote gene expression and apoptosis under 20-hydroxyecdysone regulation

Chen

Pan

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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The nuclear receptor EcRB1, which is activated by the insect steroid hormone 20-hydroxyecdysone (20E), is reportedly phosphorylated by a protein kinase after 20E induction. However, the protein kinase has not been identified, and the significance of EcRB1 phosphorylation is unclear. In this study, we identified a protein kinase C δ (PKCδ) isoform (the E isoform) that phosphorylates EcRB1 in the lepidopteran , a serious agricultural pest worldwide, to promote apoptotic gene expression and apoptosis during metamorphosis. Through activation of the EcRB1/USP1 transcription complex by 20E, expression was up-regulated in several tissues during the metamorphic stage. Knockdown of caused failure to transition from larvae to pupae, prevented tissues from undergoing programmed cell death (PCD), and down-regulated the expression of the transcription factor and the apoptosis executors and The threonine residue at position 1343 of PKCδ was phosphorylated and was critical for its proapoptotic function. Overexpression of the PKCδ catalytic domain was localized to the nuclei in HaEpi cells, which increased caspase-3 activity and apoptosis. PKCδ directly phosphorylated a threonine residue at position 468 in the amino acid sequence of EcRB1. The phosphorylation of EcRB1 was critical for its heterodimeric interaction with the USP1 protein and for binding to the ecdysone response element. The data suggested that 20E up-regulates PKCδ expression to regulate EcRB1 phosphorylation for EcRB1/USP1 transcription complex formation, apoptotic gene transcription, and apoptosis.

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“…20E triggers an intracellular calcium ion increase through an ecdysone-responsible GPCR (ErGPCR, here renamed ErGPCR1 to distinguish from ErGPCR2) (7). 20E, via G␣ q protein activation, modulates an increase of intracellular Ca 2ϩ (8). 20E regulates gene transcription via the ErGPCR, G␣ q , phospholipase C␥1, calcium, and PKC nongenomic pathway (9).…”

mentioning

confidence: 99%

The Steroid Hormone 20-Hydroxyecdysone via Nongenomic Pathway Activates Ca2+/Calmodulin-dependent Protein Kinase II to Regulate Gene Expression

Jing

Liu

Wang

et al. 2015

Journal of Biological Chemistry

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Background: 20E triggers calcium signaling to regulate 20E response gene expression. Results: 20E induces CaMKII phosphorylation and nuclear translocation, which maintains USP1 lysine acetylation by regulating HDAC3 phosphorylation and nuclear export. Conclusion: CaMKII transmits the 20E signal from cell membrane to nucleus. Significance: This study reveals that a steroid hormone, via GPCR activation and calcium signaling, regulates USP1 lysine acetylation for gene transcription.

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G-protein αq participates in the steroid hormone 20-hydroxyecdysone nongenomic signal transduction

Cited by 13 publications

References 50 publications

The Steroid Hormone 20-Hydroxyecdysone Enhances Gene Transcription through the cAMP Response Element-binding Protein (CREB) Signaling Pathway

The Steroid Hormone 20-Hydroxyecdysone Enhances Gene Transcription through the cAMP Response Element-binding Protein (CREB) Signaling Pathway

Protein kinase C delta phosphorylates ecdysone receptor B1 to promote gene expression and apoptosis under 20-hydroxyecdysone regulation

The Steroid Hormone 20-Hydroxyecdysone via Nongenomic Pathway Activates Ca2+/Calmodulin-dependent Protein Kinase II to Regulate Gene Expression

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