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Protein Kinase 휆/휄 suppresses liver cancer by repressing autophagy and oxidative phosphorylation in hepatocytes.

ABSTRACT: Protein Kinase 휆/휄 suppresses liver cancer by repressing autophagy and oxidative phosphorylation in hepatocytes.

PROVIDER: PRJNA616417 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11452807.fastq.gz	Fastqsanger.gz
	SRR11452808.fastq.gz	Fastqsanger.gz
	SRR11452809.fastq.gz	Fastqsanger.gz
	SRR11452810.fastq.gz	Fastqsanger.gz
	SRR11453510.fastq.gz	Fastqsanger.gz

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Protein Kinase / suppresses liver cancer by repressing autophagy and oxidative phosphorylation in hepatocytes [DH]

Project description:Oxidative stress plays a critical role in liver tissue damage and in hepatocellular carcinoma (HCC) initiation and progression. However, the mechanisms that regulate autophagy and metabolic reprogramming during the generation of reactive oxygen species (ROS), and how ROS promotes tumorigenesis, still need to be fully understood. We show that protein kinase C (PKC) / loss in hepatocytes promotes autophagy and oxidative phosphorylation. This results in ROS generation, which through NRF2 drives HCC cell autonomously and non-autonomously. Although PKC / promotes tumorigenesis in oncogene-driven cancer models, emerging evidence demonstrate that it is a tumor suppressor in more complex carcinogenic processes. Consistently, PKC / levels negatively correlate with HCC histological tumor grade, establishing this kinase as a tumor suppressor in liver cancer.

2020-06-30 | GSE147800 | GEO

Protein Kinase / suppresses liver cancer by repressing autophagy and oxidative phosphorylation in hepatocytes [RD]

Project description:Oxidative stress plays a critical role in liver tissue damage and in hepatocellular carcinoma (HCC) initiation and progression. However, the mechanisms that regulate autophagy and metabolic reprogramming during the generation of reactive oxygen species (ROS), and how ROS promotes tumorigenesis, still need to be fully understood. We show that protein kinase C (PKC) / loss in hepatocytes promotes autophagy and oxidative phosphorylation. This results in ROS generation, which through NRF2 drives HCC cell autonomously and non-autonomously. Although PKC/ promotes tumorigenesis in oncogene-driven cancer models, emerging evidence demonstrate that it is a tumor suppressor in more complex carcinogenic processes. Consistently, PKC / levels negatively correlate with HCC histological tumor grade, establishing this kinase as a tumor suppressor in liver cancer.

2020-06-30 | GSE147778 | GEO

Protein Kinase 휆/휄 suppresses liver cancer by repressing autophagy and oxidative phosphorylation in hepatocytes [RD]

Project description:Protein Kinase 휆/휄 suppresses liver cancer by repressing autophagy and oxidative phosphorylation in hepatocytes [RD]

| PRJNA616348 | ENA

Protein Kinase 휆/휄 suppresses liver cancer by repressing autophagy and oxidative phosphorylation in hepatocytes [DH]

Project description:Protein Kinase 휆/휄 suppresses liver cancer by repressing autophagy and oxidative phosphorylation in hepatocytes [DH]

| PRJNA616418 | ENA

Protein Kinase / suppresses liver cancer by repressing autophagy and oxidative phosphorylation in hepatocytes.

Project description:This SuperSeries is composed of the SubSeries listed below.

2020-06-30 | GSE147801 | GEO

Let-7 coordinately suppresses components of the amino acid sensing pathway to induce autophagy

Project description:Macroautophagy (hereafter autophagy) is the major pathway by which macromolecules and organelles are degraded. Autophagy is regulated by the mTOR signaling pathway, which is the focal point for integration of metabolic information, with mTORC1 playing a central role in balancing biosynthesis and catabolism. Of the various inputs to mTORC1, the amino acid sensing pathway is among the most potent. Based upon transcriptome analysis of neurons subjected to nutrient deprivation, we identified let-7 as a microRNA capable of promoting neuronal autophagy. We found that let-7 activates autophagy by coordinately down-regulating the amino acid sensing pathway to prevent mTORC1 activation. Let-7 induced autophagy in the brain and greatly reduced protein aggregates in a lentivirus model of polyglutamine disease, establishing the physiological relevance of let-7 for in vivo autophagy modulation. Moreover, peripheral delivery of let-7 anti-miR repressed autophagy in muscle and white fat, suggesting that let-7 autophagy regulation extends beyond the CNS. Hence, let-7 plays a central role in nutrient homeostasis and proteostasis regulation in higher organisms. Using sets of wild-type C57BL/6J mice, we established primary cortical neuron cultures from P0 littermates, and cultured these neurons (n = 3 / set) in CM or NLM for 4 hrs.

2015-08-03 | E-GEOD-60452 | biostudies-arrayexpress

Translational control of autophagy by Orb in the Drosophila germline [mature]

Project description:Drosophila Orb, the homologue of vertebrate CPEB is a key translational regulator involved in oocyte polarity and maturation through poly(A) tail elongation of specific mRNAs. orb has also an essential function during early oogenesis which has not been addressed at the molecular level. Here, we show that orb prevents cell death during early oogenesis, thus allowing oogenesis to progress. It does so through the repression of autophagy, by directly repressing, together with the CCR4 deadenylase, the translation of Autophagy-specific gene 12 (Atg12) mRNA. Autophagy and cell death observed in orb mutant ovaries are reduced by decreasing Atg12 or other Atg mRNA levels. These results reveal a role of Orb in translational repression and identify autophagy as an essential pathway regulated by Orb during early oogenesis. Importantly, they also establish translational regulation as a major mode of control of autophagy, a key process in cell homeostasis in response to environmental cues. Orb RIP-chip vs mock IP on ovaries from mature 3-5 day old females.

2016-07-03 | E-GEOD-74475 | biostudies-arrayexpress

Translational control of autophagy by Orb in the Drosophila germline [early]

2016-07-03 | E-GEOD-74474 | biostudies-arrayexpress

Combinatorial targeting of glycolysis and oxidative phosphorylation suppresses tumor growth and metastases.

Project description:The Warburg effect, consisting of increased glucose uptake and glycolysis, provides metabolic energy as well as cellular building blocks for tumor growth. Inhibition of the Warburg effect with 2-deoxyglucose (2DG) has been explored in clinical trials with limited efficacy. Blockage of glycolysis can induce autopahgy resulting in alternative energy generation through oxidative phosphorylation providing a potential bypass of the effects of inhibition of glycolysis. Here in we demonstrate that activation of AMPK, as a consequence of energetic stress, induces mitochondrial energy production potentially bypassing the effects of glycolysis inhibition. We thus combined blockage of glycolysis by 2DG with inhibition of the electron transfer complex I (ETC1) in the mitochondria with the clinically applicable antidiabetic drug metformin. The combination resulted in activation of AMPK and autopahgy that however rendered eventual depletion of ATP and cell death. Furthermore, combined inhibition of glycolysis and mitochondrial respiration inhibited tumor growth and markedly decreased metastatic capacity in vivo. In order to understand the mechanism of these metabolic inhibitors, we performed whole genome transcriptional analysis. Human SK-4 esophageal cancer cell lines were treated with 5 different treatment groups [2 deoxy glucose (4mM), Metformin (5mM), AICAR (2mM), 2 deoxy glucose (4mM) plus Metformin (5mM) and 2 deoxy glucose (4mM) plus AICAR (2mM)] with non treated control groups for 12 hrs. Each groups was quadruplicated. Microarray experiments and data analysis were done at Dept. of Systems Biology, MDACC (Houston, USA)

2012-12-31 | E-GEOD-16816 | biostudies-arrayexpress

Casein kinase II suppresses autophagy by activating Filamin-NHL containing TRIM proteins

Project description:Autophagy is a tightly regulated process integral to cellular homeostasis and innate immunity. As such, dysregulation of autophagy is associated with cancer, neurodegenerative disorders, and infectious diseases. While many factors have been characterized that promote autophagy, key players preventing excessive autophagy are less well understood. Here, we identify Casein kinase II (CK2) as a negative regulator of autophagy. Pharmacological inhibition of CK2 activity or siRNA-mediated depletion of CK2 increased basal autophagic flux in cell lines and primary human lung cells. Vice versa, ectopic expression of CK2 reduced autophagic flux. Mechanistically, CK2 interacts with tripartite motif (TRIM) family members TRIM2, TRIM3 and TRIM71 at their shared C-terminal NHL domain. This interaction was required for autophagy inhibition by CK2. TRIM3 was highly phosphorylated by CK2 at serine 661, and a phosphorylation-defective mutant of TRIM3 was unable to reduce autophagy induction. Targeting of the CK2-TRIM axis promoted autophagy during influenza A virus (IAV) and measles virus (MeV) infection. In line with this, inhibition of CK2 enhanced autophagy-dependent restriction of IAV, MeV and human immunodeficiency virus 1 (HIV-1). Thus, our results identify the CK2-TRIM2/3/71 axis as a key regulatory pathway that limits autophagy. Targeting this axis may allow therapeutic induction of autophagy against viral infections and diseases associated with dysregulated autophagy.

2023-05-16 | MSV000091956 | MassIVE

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