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Role of the metabolic sensor AMP-activated protein kinase in T cell function in vivo [RNA-seq]

ABSTRACT: Role of the metabolic sensor AMP-activated protein kinase in T cell function in vivo [RNA-seq]

PROVIDER: PRJNA638419 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR11969138.fastq.gz	Fastqsanger.gz
	SRR11969139.fastq.gz	Fastqsanger.gz
	SRR11969140.fastq.gz	Fastqsanger.gz
	SRR11969141.fastq.gz	Fastqsanger.gz
	SRR11969142.fastq.gz	Fastqsanger.gz

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Role of the metabolic sensor AMP-activated protein kinase in T cell function in vivo

Project description:Role of the metabolic sensor AMP-activated protein kinase in T cell function in vivo

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Role of the metabolic sensor AMP-activated protein kinase in T cell function in vivo [TCR-seq]

Project description:Role of the metabolic sensor AMP-activated protein kinase in T cell function in vivo [TCR-seq]

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The yeast AMP-activated protein kinase Snf1p phosphorylates the inositol polyphosphate kinase Kcs1p

Project description:The yeast AMP-activated protein kinase Snf1p phosphorylates the inositol polyphosphate kinase Kcs1p

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The γ2 subunit of AMP-activated protein kinase regulates mammalian heart rate

Project description:AMP-activated protein 1 kinase (AMPK), a phylogenetically conserved serine/threonine kinase regarded as a key cellular energy sensor, exists in eukaryotes as a heterotrimer comprising a catalytic α and regulatory β and γ subunits. In humans, activating mutations in the gene encoding the γ2 subunit of AMPK (PRKAG2) display a cardiac phenotype of left ventricular hypertrophy (LVH), conduction system disease, ventricular pre-excitation and increased cardiomyocyte glycogen accumulation. While existing transgenic models have elucidated the pathogenesis of several aspects of the disease5-7, the slow heart rate (sinus bradycardia) – a prominent feature of the disease – remains poorly understood. Here, using gene-targeting to generate mice which recapitulate this bradycardia, we demonstrate that γ2 AMPK activation perturbs fundamental mechanisms that determine sinoatrial pacemaker cell function. Reduction in the sarcolemmal hyperpolarization activated (“funny”) current (If) and damping of ryanodine receptor-derived diastolic local subsarcolemmal Ca2+ releases (LCRs)12,13 contribute to reduced sinoatrial cell spontaneous activity and, ultimately, to a lower heart rate. Pharmacological activation of AMPK reversibly reduces the beating rate of murine pluripotent stem cell-derived induced sinoatrial bodies. In contrast, using a mouse knock-out of γ2 AMPK, which exhibits an increased heart rate, we demonstrate a role for γ2 AMPK in physiological heart rate regulation, including an indispensable role in the bradycardic adaptation to endurance exercise. Through regulating the cardiac pacemaker and thereby heart rate, γ2 AMPK by virtue of its energy-sensing role, is a key physiological determinant of overall cardiac energy homeostasis.

2017-09-30 | GSE73047 | GEO

Biosacetalin 1,1-Diethoxyethane enhances aerobic respiration via activation of AMP-activated protein kinase

Project description:Biosacetalin 1,1-Diethoxyethane enhances aerobic respiration via activation of AMP-activated protein kinase

| PRJNA1425579 | ENA

Role of the metabolic sensor AMP-activated protein kinase in T cell function in vivo

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

2021-06-04 | GSE152157 | GEO

The yeast AMP-activated protein kinase Snf1p phosphorylates the inositol polyphosphate kinase Kcs1p

Project description:The yeast Snf1p/AMP-activated kinase (AMPK) maintains energy homeostasis, controlling metabolic processes and glucose derepression in response to nutrient levels and environmental cues. Under conditions of nitrogen or glucose limitation, Snf1p regulates pseudohyphal growth, a morphological transition characterized by the formation of extended multicellular filaments. During pseudohyphal growth, Snf1p is required for wild-type levels of inositol polyphosphate (InsP), soluble phosphorylated species of the six-carbon cyclitol inositol that function as conserved metabolic second messengers. InsP levels are established through the activity of a family of inositol kinases, including the inositol polyphosphate kinase Kcs1p, which principally generates pyrophosphorylated forms of InsP7 and InsP8. Here, we report that Snf1p regulates Kcs1p, affecting Kcs1p phosphorylation and inositol kinase activity. A snf1 kinase-defective mutant exhibits decreased Kcs1p phosphorylation, and Kcs1p is phosphorylated in vivo at Ser residues 537 and 646 during pseudohyphal growth. By in vitro analysis, Snf1p directly phosphorylates Kcs1p, predominantly at amino acids 537 and 646. A yeast strain carrying kcs1 encoding Ser-to-Ala point mutations at these residues (kcs1-S537A,S646A) shows elevated levels of pyrophosphorylated InsP7, comparable to InsP7 levels observed upon deletion of SNF1. The kcs1-S537A,S646A mutant exhibits decreased pseudohyphal growth, invasive growth, and cell elongation. Transcriptional profiling indicates extensive perturbation of metabolic pathways in kcs1-S537A,S646A. Growth of kcs1-S537A,S646A is affected on medium containing glycerol and antimycin A, consistent with decreased Snf1p signaling. This work identifies Snf1p phosphorylation of Kcs1p, collectively highlighting the interconnectedness of AMPK activity and InsP signaling in coordinating nutrient availability, energy homoeostasis, and cell growth.

2024-01-10 | GSE246711 | GEO

Biosacetalin 1,1-Diethoxyethane enhances aerobic respiration via activation of AMP-activated protein kinase

Project description:The enzyme 5ʹ-adenosine monophosphate (AMP)-activated protein kinase (AMPK) is a key regulator of cellular energy metabolism, playing a protective role in cardiovascular remodeling and diseases. Here, 1,1-Diethoxyethane (1,1-DEE), a compound traditionally known as a flavoring agent in wine and distilled spirits, was identified as an AMPK activator. By analyzing AC16 cardiomyocytes with the Seahorse Mito Stress Test, we found that 1,1-DEE induced a transient inhibition of both mitochondrial respiration and glycolysis, resulting in reduced ATP production. This metabolic disturbance triggered AMPK activation in a time- and concentration-dependent manner, leading to adaptive increases in the phosphorylation of acetyl-CoA carboxylase and 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2, which promotes fatty acid oxidation and glycolysis. AMPK activation also enhanced mitochondrial biogenesis by upregulating peroxisome proliferator-activated receptor gamma coactivator 1-alpha and mitochondrial transcription factor A. These alterations led to a sustained increase in both mitochondrial respiration and glycolysis. Overall, our findings unravel the important physiological role of 1,1-DEE in energy homeostasis through AMPK activation and aerobic respiration. This mechanism may hold therapeutic potential for the prevention and treatment of metabolic and cardiovascular diseases.

2026-02-19 | GSE319948 | GEO

Protein Kinase AMP-Activated Catalytic Subunit Alpha 1 (PRKAA1) knockdown effect on the transcriptome of primary human acute myeloid leukemia (AML) cells

Project description:To explore the function of AMPK signaling in acute myeloid leukemia (AML), we used shRNA to knock down the expression of PRKAA1, the catalytic subunit of the 5'-prime-AMP-activated protein kinase (AMPK), in primary human AML cells and performed RNA-seq experiment to profile transcriptional changes upon AMPK inactivation.

2018-06-01 | GSE114105 | GEO

Role of the metabolic sensor AMP-activated protein kinase in T cell function in vivo [TCR-seq]

Project description:Purpose: To investigate the function of AMPK in T cells during in vivo activation. Methods: WT (PRKAA1fl/fl) and KO (CD4-Cre PRKAA1fl/fl) T cells were transferred into Rag KO recipients to induce adoptive T cell transfer mediated colitis. Donor WT and KO spleen and mLN T cells were isolated 6 weeks after transfer and gene expression was assessed in WT vs. KO T cells and spleen vs. mLN samples.

2021-06-04 | GSE152156 | GEO

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