A novel light-dependent activation of DAGK and PKC in bovine photoreceptor nuclei

Natalini, Paola M.; Mateos, Melina Valeria; Boschero, Mónica G. Ilincheta de; Giusto, Norma M.

doi:10.1016/j.exer.2014.06.007

Cited by 5 publications

(17 citation statements)

References 64 publications

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“…By contrast, histamine binding to H2R activates protein kinase A (PKA) and binds cAMP via adenylate cyclase 43 to suppress MAP kinase activation. Instead, H1R signaling involves the conversion of phosphatidylinositol 2 (PIP2) by phospholipase C (PLC) into diacylglycerol (DAG) and inositol triphosphate (IP3) 25 , 43 , 44 . DAG stimulates phosphorylation of protein kinase C (PKC) 5 , 23 , 44 by binding to the catalytic domain 1 and recruiting PKC to the membrane.…”

Section: Discussionmentioning

confidence: 99%

“…Instead, H1R signaling involves the conversion of phosphatidylinositol 2 (PIP2) by phospholipase C (PLC) into diacylglycerol (DAG) and inositol triphosphate (IP3) 25 , 43 , 44 . DAG stimulates phosphorylation of protein kinase C (PKC) 5 , 23 , 44 by binding to the catalytic domain 1 and recruiting PKC to the membrane. The interaction of PKC with the membrane causes release of pseudosubstrate from the catalytic domain leading to availability of serine, threonine phosphoacceptor residues causing PKC activation 45 .…”

Section: Discussionmentioning

confidence: 99%

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Diacylglycerol kinase synthesized by commensal Lactobacillus reuteri diminishes protein kinase C phosphorylation and histamine-mediated signaling in the mammalian intestinal epithelium

et al. 2018

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Lactobacillus reuteri 6475 (Lr) of the human microbiome synthesizes histamine and can suppress inflammation via type 2 histamine receptor (H2R) activation in the mammalian intestine. Gut microbes such as Lr promote H2R signaling and may suppress H1R pro-inflammatory signaling pathways in parallel by unknown mechanisms. In this study, we identified a soluble bacterial enzyme known as diacylglycerol kinase (Dgk) from Lr that is secreted into the extracellular milieu and presumably into the intestinal lumen. DgK diminishes diacylglycerol (DAG) quantities in mammalian cells by promoting its metabolic conversion and causing reduced PKC phosphorylation (pPKC) as a net effect in mammalian cells. We demonstrated that histamine synthesized by gut microbes (Lr) activates both mammalian H1R and H2R, but Lr-derived Dgk suppresses the H1R signaling pathway. Phospho-PKC and IκBα were diminished within the intestinal epithelium of mice and humans treated by WT Lr, but pPKC and IκBα were not decreased in treatment with ΔdgkA Lr. Mucosal IL-6 and systemic IL-1α, eotaxin and G-CSF were suppressed in WT Lr, but not in ΔdgkA Lr colonized mice. Collectively, the commensal microbe Lr may act as a “microbial antihistamine” by suppressing intestinal H1R mediated pro-inflammatory responses via diminished pPKC-mediated mammalian cell signaling.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Diacylglycerol kinase synthesized by commensal Lactobacillus reuteri diminishes protein kinase C phosphorylation and histamine-mediated signaling in the mammalian intestinal epithelium

et al. 2018

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“…DAG is an important signaling second messenger in cells, contributing to the activity of PKC isoforms among other functions. 108 – 111 In addition to its function as a second messenger, DAG is a precursor for phosphatidic acid (PA), which exhibits mitogenic properties contributing to the activation of Ras downstream of receptor tyrosine kinase engagement 112 , 113 and thereby contributing to MAPK signaling. 18 , 114 PA also triggers mTOR activation through direct binding and activation of Akt 18 , 115 – 117 ( Figure 3 ).…”

Section: Perk Substratesmentioning

confidence: 99%

Tumor progression and the different faces of the PERK kinase

2015

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The serine/threonine endoplasmic reticulum (ER) kinase, protein kinase R (PKR)-like endoplasmic reticulum kinase (PERK), is a pro-adaptive protein kinase whose activity is regulated indirectly by protein misfolding within the ER. Since the oxidative folding environment in the ER is sensitive to a variety of cellular stresses, many of which occur during neoplastic transformation and in the tumor microenvironment, there has been considerable interest in defining whether PERK positively contributes to tumor progression and whether it represents a significant therapeutic target. Herein, we review the current knowledge of PERK-dependent signaling pathways, the contribution of downstream substrates including recently characterized new PERK substrates transcription factors FOXO (Forkhead box O protein) and diacyglycerol (DAG) a lipid signaling second messenger, and efforts to develop small molecule PERK inhibitors.

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“…This phenomena might be due to the fact that other subtypes of PKC play an important role in retina function, such as aPKCζ , 44,45 nPKCδ, 44,46 and cPKCα. 47,48 In addition, the intraocular pressures of the MD and control eyes were 8.67 ± 0.380 mm Hg and 8.5 ± 0.365 mm Hg, respectively (n = 6 per group; t = 0.316; degrees of freedom = 10; P = 0.758). Other reasons for the drop in ERG amplitudes might be temporary impairment of retinal function, 42 as well as the reduction of ganglion, inner nuclear, and outer nuclear cells 49 ; axial elongation of eye 50 ; and ischemic insult 51 in the deprived eye.…”

Section: Discussionmentioning

confidence: 94%

Monocular Deprivation Affects Visual Cortex Plasticity Through cPKCγ-Modulated GluR1 Phosphorylation in Mice

Zhang

Han

et al. 2020

Invest. Ophthalmol. Vis. Sci.

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Purpose To determine how visual cortex plasticity changes after monocular deprivation (MD) in mice and whether conventional protein kinase C gamma (cPKCγ) plays a role in visual cortex plasticity. Methods cPKCγ membrane translocation levels were quantified by using immunoblotting to explore the effects of MD on cPKCγ activation. Electrophysiology was used to record field excitatory postsynaptic potential (fEPSP) amplitude with the goal of observing changes in visual cortex plasticity after MD. Immunoblotting was also used to determine the phosphorylation levels of GluR1 at Ser831. Light transmission was analyzed using electroretinography to examine the effects of MD and cPKCγ on mouse retinal function. Results Membrane translocation levels of cPKCγ significantly increased in the contralateral visual cortex of MD mice compared to wild-type (WT) mice ( P < 0.001). In the contralateral visual cortex, long-term potentiation (LTP) and the phosphorylation levels of GluR1 at Ser 831 were increased in cPKCγ +/+ mice after MD. Interestingly, these levels could be downregulated by cPKCγ knockout compared to cPKCγ +/+ +MD mice ( P < 0.001). Compared to the right eyes of WT mice, the amplitudes of a-waves and b-waves declined in deprived right eyes of mice after MD ( P < 0.001). There were no significant differences when comparing cPKCγ +/+ and cPKCγ −/− mice with MD. Conclusions cPKCγ participates in the plasticity of the visual cortex after MD, which is characterized by increased LTP in the contralateral visual cortex, which may be a result of cPKCγ-mediated phosphorylation of GluR1 at Ser 831.

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A novel light-dependent activation of DAGK and PKC in bovine photoreceptor nuclei

Cited by 5 publications

References 64 publications

Diacylglycerol kinase synthesized by commensal Lactobacillus reuteri diminishes protein kinase C phosphorylation and histamine-mediated signaling in the mammalian intestinal epithelium

Diacylglycerol kinase synthesized by commensal Lactobacillus reuteri diminishes protein kinase C phosphorylation and histamine-mediated signaling in the mammalian intestinal epithelium

Tumor progression and the different faces of the PERK kinase

Monocular Deprivation Affects Visual Cortex Plasticity Through cPKCγ-Modulated GluR1 Phosphorylation in Mice

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