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Role of p110a subunit of PI3-kinase in skeletal muscle mitochondria

ABSTRACT: Role of p110a subunit of PI3-kinase in skeletal muscle mitochondria

PROVIDER: PRJNA511896 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR8370620_1.fastq.gz	Fastqsanger.gz
	SRR8370620_2.fastq.gz	Fastqsanger.gz
	SRR8370630_1.fastq.gz	Fastqsanger.gz
	SRR8370630_2.fastq.gz	Fastqsanger.gz
	SRR8370640_1.fastq.gz	Fastqsanger.gz

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Role of p110a subunit of PI3-kinase in skeletal muscle mitochondria

Project description:Skeletal muscle insulin resistance, decreased phosphatidylinositol 3-kinase (PI3K) activation and altered mitochondrial function are hallmarks of type 2 diabetes. We created mice with a muscle-specific knockout of p110α or p110β, the two major catalytic subunits of PI3K. We find that mice with muscle-specific knockout of p110α, but not p110β, display impaired muscle insulin signaling and reduced muscle size due to enhanced proteasomal and autophagic activity. Despite insulin resistance and muscle atrophy, M-p110αKO mice show decreased serum myostatin, increased mitochondrial mass, increased mitochondrial fusion visualized by intravital microscopy, and increased PGC1α expression, especially PCG1α2 and PCG1α3. This leads to enhanced mitochondrial oxidative capacity, striking increases in muscle NADH content, and higher muscle free radical release measured in vivo using pMitoTimer reporter. Thus, p110α is the dominant catalytic isoform of PI3K in muscle in control of insulin sensitivity and muscle mass, and has a unique role in mitochondrial homeostasis in skeletal muscle.

2019-03-12 | GSE124394 | GEO

RAS signalling through PI3-Kinase controls cell migration via modulation of Reelin expression

2016-02-12 | GSE77843 | GEO

RAS signalling through PI3-Kinase controls cell migration via modulation of Reelin expression

Project description:RAS signalling through Phosphoinositide 3-kinase (PI3-Kinase) has been shown to have an essential role in tumour initiation and maintenance. RAS also regulates cell motility and tumor invasiveness, but the role of direct RAS binding to PI3-Kinase in this remains uncertain. Here, we provide evidence that disruption of RAS interaction with PI3-Kinase p110adecreases cell motility and prevents activation of Rac GTPase. Analysis of gene expression in cells lacking RAS interaction with p110areveals increased levels of the extracellular matrix glycoprotein ReelinÂ and activation of its downstream pathway resulting in upregulation of E-Cadherin expression. Induction of the Reelin / E-Cadherin axis is also observed in Kras mutant lung tumours that are regressing due to blockade of RAS interaction with PI3-Kinase. Furthermore, loss of Reelin correlates with decreasedÂ survival of lung and breast cancer patients.Â Reelin thus plays a role in restraining RAS and PI3-kinase promotion of cell motility and potentially tumour metastasis. MEFs with or without RAS binding to p110a were seeded in a 10cm dish and left to attach during 24 hours. Full serum media was then removed and media with no FBS was added to the plates. Starvation was carried out during a period of 16 hours (over night starvation). Assay was performed in triplicates: for each genotype two diferent fibroblasts clones (and a mix of both of the clones) were used on the analysis. After starvation RNA was extracted using RNAsy kit (Quiagen). RNA was quantified and sent to Oxford Gene Technology microarray facility.

2016-02-12 | E-GEOD-77843 | biostudies-arrayexpress

Gene expression changes upon treatment of T47D breast cancer cells with the Pan-PI3 kinase inhibitor GDC-0941

Project description:We sought to determine genes whose expression changed upon treatment with a selective inhibitor of class I PI3 kinase.

2010-05-25 | GSE20719 | GEO

Gene expression changes upon treatment of T47D breast cancer cells with the Pan-PI3 kinase inhibitor GDC-0941

Project description:We sought to determine genes whose expression changed upon treatment with a selective inhibitor of class I PI3 kinase. Total of 6 samples: cells were treated with GDC-0941 at a concentration of 1mM for 6 hours (3 replicates) and control (3 replicates)

2010-06-08 | E-GEOD-20719 | biostudies-arrayexpress

Micro RNA expression in rodent skeletal muscle mitochondria

Project description:Micro RNA expression in rodent skeletal muscle mitochondria

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Role of p110a subunit of PI3-kinase in skeletal muscle mitochondrial homeostasis and metabolism.

Project description:Skeletal muscle insulin resistance, decreased phosphatidylinositol 3-kinase (PI3K) activation and altered mitochondrial function are hallmarks of type 2 diabetes. To determine the relationship between these abnormalities, we created mice with muscle-specific knockout of the p110α or p110β catalytic subunits of PI3K. We find that mice with muscle-specific knockout of p110α, but not p110β, display impaired insulin signaling and reduced muscle size due to enhanced proteasomal and autophagic activity. Despite insulin resistance and muscle atrophy, M-p110αKO mice show decreased serum myostatin, increased mitochondrial mass, increased mitochondrial fusion, and increased PGC1α expression, especially PCG1α2 and PCG1α3. This leads to enhanced mitochondrial oxidative capacity, increased muscle NADH content, and higher muscle free radical release measured in vivo using pMitoTimer reporter. Thus, p110α is the dominant catalytic isoform of PI3K in muscle in control of insulin sensitivity and muscle mass, and has a unique role in mitochondrial homeostasis in skeletal muscle.

| S-EPMC6667496 | biostudies-literature

Mutationally-activated PI3’-kinase-a promotes de-differentiation of lung tumors initiated by the BRAFV600E oncoprotein kinase

Project description:Mutationally-activated PI3’-kinase-a promotes de-differentiation of lung tumors initiated by the BRAFV600E oncoprotein kinase

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Purification of mitochondria from skeletal muscle tissue for transcriptomic analyses reveals localization of nuclear-encoded non-coding RNAs [SMvsMT]

Project description:Mitochondria are central to cellular function, particularly in metabolically active tissues such as skeletal muscle. Nuclear-encoded RNAs typically localise within the nucleus and cytosol but a small population may also translocate to subcellular compartments such as mitochondria. We aimed to investigate the nuclear-encoded RNAs that localise within the mitochondria of skeletal muscle tissue. Intact mitochondria were isolated via immunoprecipitation (IP) followed by enzymatic treatments (RNase-A and proteinase-K) optimised to remove transcripts located exterior to mitochondria, making it amenable for high-throughput transcriptomic sequencing. Whole-transcriptome RNA sequencing of enzymatically-purified mitochondria isolated by IP from skeletal muscle tissue showed a high degree of purity. In summary, we describe a novel, powerful sequencing approach applicable to animal and human tissues and cells that can facilitate the discovery of nuclear-encoded RNA transcripts localised within skeletal muscle mitochondria.

2024-09-11 | GSE276307 | GEO

Purification of mitochondria from skeletal muscle tissue for transcriptomic analyses reveals localization of nuclear-encoded non-coding RNAs [Mitoplasts]

Project description:Mitochondria are central to cellular function, particularly in metabolically active tissues such as skeletal muscle. Nuclear-encoded RNAs typically localise within the nucleus and cytosol but a small population may also translocate to subcellular compartments such as mitochondria. We aimed to investigate the nuclear-encoded RNAs that localise within the mitochondria of skeletal muscle cells and tissue. Intact mitochondria were isolated via immunoprecipitation (IP) followed by enzymatic treatments (RNase-A and proteinase-K) to remove transcripts located exterior to mitochondria, making it amenable for high-throughput transcriptomic sequencing. Whole-transcriptome RNA sequencing of enzymatically-purified mitochondria isolated by IP from skeletal muscle tissue showed a striking similarity in the degree of purity compared to mitoplast preparations which lack an outer mitochondrial membrane. In summary, we describe a novel, powerful sequencing approach applicable to animal and human tissues and cells that can facilitate the discovery of nuclear-encoded RNA transcripts localised within skeletal muscle mitochondria.

2024-09-11 | GSE276306 | GEO

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