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Phosphorylation of TET2 by AMPK is indispensable in myogenic differentiation

ABSTRACT: Phosphorylation of TET2 by AMPK is indispensable in myogenic differentiation

PROVIDER: PRJNA521716 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR8556640_1.fastq.gz	Fastqsanger.gz
	SRR8556640_2.fastq.gz	Fastqsanger.gz
	SRR8556660_1.fastq.gz	Fastqsanger.gz
	SRR8556660_2.fastq.gz	Fastqsanger.gz
	SRR8556670_1.fastq.gz	Fastqsanger.gz

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Phosphorylation of TET2 by AMPK is indispensable in myogenic differentiation [RNA-seq]

Project description:Phosphorylation of TET2 by AMPK is indispensable in myogenic differentiation [RNA-seq]

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Phosphorylation of TET2 by AMPK is indispensable in myogenic differentiation [MeDIP-seq]

Project description:Phosphorylation of TET2 by AMPK is indispensable in myogenic differentiation [MeDIP-seq]

| PRJNA521719 | ENA

Phosphorylation of TET2 by AMPK is indispensable in myogenic differentiation [RNA-seq]

Project description:TET-mediated oxidation of 5-mC participates in both passive and active DNA demethylation, which exerts a significant influence on diverse biological processes. Mass spectrometry has identified multiple phosphorylation sites of TET2. However, the functions of these phosphosites and their corresponding kinases are mostly unknown. Here we showed that AMP-activated protein kinase (AMPK) phosphorylates murine TET2 at the serine residue 97 (S97), enhances TET2 stability through promoting its binding to 14-3-3β. AMPK ablation resulted in decreased global 5-hmC levels at the myotube stages, severe differentiation defects of C2C12 cells and, significantly, total loss of expression of Pax7. Genome-wide analyses revealed increased DNA methylation at genic and enhancer regions of AMPK-null myoblasts and myotubes. Using CRISPR/Cas9 technology, we showed that a novel enhancer, which is hypermethylated in AMPK-null cells, regulates Pax7 expression. The phospho-mimicking mutant, TET2-S97E, could partly rescue the differentiation defect in AMPK ablated C2C12 cells. Together, our data demonstrated that AMPK is a critical regulator of myogenesis, partly through phosphorylating TET2.

2019-06-06 | GSE126370 | GEO

Phosphorylation of TET2 by AMPK is indispensable in myogenic differentiation [MeDIP-seq]

2019-06-06 | GSE126369 | GEO

Phosphorylation of TET2 by AMPK is indispensable in myogenic differentiation.

Project description:BackgroundTET-mediated oxidation of 5-mC participates in both passive and active DNA demethylation, which exerts a significant influence on diverse biological processes. Mass spectrometry has identified multiple phosphorylation sites of TET2. However, the functions of these phosphosites and their corresponding kinases are mostly unknown.ResultsHere, we showed that AMP-activated protein kinase (AMPK) phosphorylates murine TET2 at the serine residue 97 (S97), and the phosphorylation enhances TET2 stability through promoting its binding to 14-3-3β. AMPK ablation resulted in decreased global 5-hmC levels at the myotube stages, severe differentiation defects of C2C12 cells and significantly, total loss of expression of Pax7. Genome-wide analyses revealed increased DNA methylation at genic and enhancer regions of AMPK-null myoblasts and myotubes. Using CRISPR/Cas9 technology, we showed that a novel enhancer, which is hypermethylated in AMPK-null cells, regulates Pax7 expression. The phospho-mimicking mutant, TET2-S97E, could partly rescue the differentiation defect in AMPK-ablated C2C12 cells.ConclusionsTogether, our data demonstrated that AMPK is a critical regulator of myogenesis, partly through phosphorylating TET2.

| S-EPMC6547497 | biostudies-literature

14-3-3 protects AMPK phosphorylated TET2 from dephosphorylation by PP2A

Project description:Ten-eleven translocation-2 (TET2) is a member of the methylcytosine dioxygenase family of enzymes implicated in cancer and in aging due to its role as a global epigenetic modifier. TET2 has a large N-terminal domain followed by a catalytic C-terminal. Previous reports have demonstrated that the catalytic domain remains active independent of the N-terminal domain. As such, the function of the N-terminus of this large protein remains poorly characterized. Here, we identify that several isoforms of the 14-3-3 family of proteins bind TET2. 14-3-3s bind TET2 when phosphorylated at serine 99 (S99). AMPK-mediated phosphorylation at S99 promotes TET2 stability and increases global DNA 5-hydroxymethylcytosine. 14-3-3s’ interaction with TET2 serves to protect S99 phosphorylation. Disruption of this interaction leads to both reduced TET2 phosphorylation and decreased protein stability. Furthermore, we identify that the protein phosphatase 2A (PP2A) can interact with TET2 and dephosphorylates S99. Collectively, our study provides novel insights into the role of the N-terminal domain in TET2 regulation. Moreover, they demonstrate the dynamic nature of TET2 protein regulation that could have therapeutic implications for disease states resulting from reduced TET2 levels and/or activity.

2020-01-13 | PXD016160 | Pride

Phosphorylation of TET2 by AMPK is indispensable in myogenic differentiation

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

2019-06-06 | GSE126371 | GEO

VRK-1 Extends Lifespan by Activation of AMPK via Phosphorylation

Project description:Vaccinia virus-related kinase (VRK) is an evolutionarily conserved nuclear protein kinase. VRK-1, the single Caenorhabditis elegans VRK ortholog, functions in cell division and germline proliferation. However, the role of VRK-1 in post-mitotic cells and adult lifespan remain unknown. Here, we show that VRK-1 increases organismal longevity by activating the cellular energy sensor, AMP-activated protein kinase (AMPK), via direct phosphorylation. We found that overexpression of vrk-1 in the soma of adult C. elegans increased lifespan, and conversely, inhibition of vrk-1 decreased lifespan. In addition, vrk-1 was required for longevity conferred by mutations that inhibit C. elegans mitochondrial respiration, which requires AMPK. Notably, VRK-1 directly phosphorylated and up-regulated AMPK in both C. elegans and cultured human cells. Thus, our data show that the somatic nuclear kinase, VRK-1, promotes longevity through AMPK activation, and this function appears to be conserved between C. elegans and humans.

2020-07-01 | GSE138129 | GEO

VRK-1 Extends Lifespan by Activation of AMPK via Phosphorylation

Project description:VRK-1 Extends Lifespan by Activation of AMPK via Phosphorylation

| PRJNA574844 | ENA

Jak2 mediated phosphorylation and activation of TET2 in hematopoiesis

Project description:Jak2 mediated phosphorylation and activation of TET2 in hematopoiesis

| PRJNA478948 | ENA