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The hepatic overexpression of C2-AKT ameliorates obesity-induced insulin resistance

ABSTRACT: The hepatic overexpression of C2-AKT ameliorates obesity-induced insulin resistance

PROVIDER: PRJNA1146934 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR30205841_1.fastq.gz	Fastqsanger.gz
	SRR30205841_2.fastq.gz	Fastqsanger.gz
	SRR30205842_1.fastq.gz	Fastqsanger.gz
	SRR30205842_2.fastq.gz	Fastqsanger.gz
	SRR30205843_1.fastq.gz	Fastqsanger.gz

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The hepatic overexpression of C2-AKT ameliorates obesity-induced insulin resistance

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Akt phosphorylates insulin receptor substrate (IRS) to limit PI3K-mediated PI(3,4,5)P3 synthesis

Project description:The phosphoinositide 3-kinase (PI3K)-Akt network is tightly controlled by feedback mechanisms that regulate signal flow and ensure signal fidelity. Here, we show that Akt itself engages negative feedback by phosphorylating insulin receptor substrate (IRS) 1 and 2 on a number of residues. Mechanistically this serves to deplete plasma membrane-localised IRS1/2 and reduce its interaction with the insulin receptor. Together these events limit plasma membrane associated PI3K and phosphatidylinositol (3,4,5)-trisphosphate (PIP3) synthesis. We identified two Akt-dependent phosphorylation sites in IRS2 at S306 (S303 in mouse) and S577 (S573 in mouse) that are key drivers of this negative feedback. These findings establish another mechanism by which the kinase Akt auto-regulates its activity, through post-translational modification of the IRS scaffold that in turn controls PIP3 levels.

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Phosphoproteomics of consecuively active AKT in liver and Insulin stimulated primary Hepatocytes

Project description:Liver mitochondria play a central role in metabolic adaptations to changing nutritional states, yet their dynamic regulation upon anticipated changes in the energy state has remained unaddressed. Here, we show that sensory food perception rapidly induces mitochondrial fission in the liver via protein kinase B/AKT-dependent phosphorylation of serine 131 of the Mitochondrial fission factor (MFFS131), a response mediated via activation of hypothalamic Pro-opiomelanocortin (POMC)-expressing neurons. A non-phosphorylatable MFFS131G knock-in mutation abrogates AKT-induced mitochondrial fragmentation in vitro. In vivo, MFFS131G knock-in mice display altered liver mitochondrial dynamics upon refeeding and impaired insulin stimulated suppression of gluconeogenesis. Collectively, we reveal a critical role for rapid activation of a hypothalamic/liver axis to adapt mitochondrial function to anticipated changes of nutritional state in control of hepatic glucose metabolism. R26-fl-Akt-C mice Mice carrying a conditional myristoylation tagged Akt-C transgene in the ROSA26 locus were used to activate AKT in the liver with a liver specific Cre-dependent virus. The generation of this line has been described previously (V. Kohlhaas et al, 2021) For AAV mediated liver-specific delivery of Cre, R26-fl-Akt-C or control mice were injected with a AAV8-TBG-iCre virus (VB1724, Vector Biolabs). This repository contains two experiments a) Liver of liver active Akt-CA and b) Insulin stimulation of primary heptocytes. Please note that replicate one of the hepatocyte dataset have been removed from the analysis due to the limited number of posphosites compared to others.

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