MétaCan
← all works

PGC‐1α gene expression is down‐regulated by Akt‐mediated phosphorylation and nuclear exclusion of FoxO1 in insulin‐stimulated skeletal muscle

2005· article· en· 73 citations· W2162645376 on OpenAlex· 10.1096/fj.05-3993fje

Why is this work in the frame?

A frame that forgets how it found something cannot be audited. These are the routes that admitted this work.

Canadian funderA Canadian agency funded it. The work may carry no Canadian affiliation at all.

No Canadian affiliation. An affiliation-only frame — the usual design — would never have seen this work. It is one of the works that make the case for inverting the frame.

Post-publication record

Nature
Retraction
Reason
Concerns/Issues about Results and/or Conclusions;Investigation by Company/Institution;Investigation by Third Party;
Date
7/29/2009 0:00
Flagged by OpenAlex?
Yes

Source: Retraction Watch, joined by DOI. OpenAlex records retraction as is_retracted, a boolean over a state space with at least four values, so it cannot express an expression of concern, a correction or a reinstatement — it reports them as false, which reads as “fine”.

Abstract

There are multiple binding domains on the promoter region of the peroxisome proliferator activator receptor gamma coactivator-1 alpha (PGC-1alpha) gene, including a trio of insulin responsive elements that are activated by the forkhead box class-O (FoxO1) winged helix transcription factor, which is known to be regulated by acute transforming retrovirus thymoma (Akt). Here we show that in skeletal muscle biopsy specimens from healthy humans and cultured human skeletal myotubes, insulin phosphorylates Akt (Ser473) and FoxO1 (Thr24, Ser256), leading to reduced nuclear abundance of FoxO1 total protein. This is associated with an insulin-mediated repression of the mRNA expression PGC-1alpha and downstream genes associated with oxidative phosphorylation. In contrast, in muscle taken from insulin resistant humans or in palmitate-treated insulin resistant myotubes, neither Akt nor FoxO1 was phosphorylated by insulin, resulting in a failure for nuclear exclusion of FoxO1 total protein, and an inability for insulin to repress the mRNA expression of PGC-1alpha and down-stream genes. To determine whether the regulation of FoxO1 was Akt dependent, we next treated Akt2 -/- and wild-type mice with or without insulin. Insulin phosphorylated Akt and FoxO1 (Thr24, Ser256) resulting in a reduced nuclear expression of FoxO1 total protein in wild-type but not Akt2 -/- skeletal muscle. We conclude that insulin decreases the expression of genes involved in oxidative metabolism in healthy but not insulin resistant muscle, due to a decrease in FoxO1 phosphorylation and nuclear exclusion secondary to reduced Akt activity.

Fetched live from OpenAlex and de-inverted. Abstracts are not stored in this database: the inverted indexes are 8.6 GB of the frame’s 9.3 GB of text, and the host has 13 GB free.

The record

Venue
The FASEB Journal
Topic
FOXO transcription factor regulation
Field
Biochemistry, Genetics and Molecular Biology
Canadian institutions
Funders
Division of Arctic SciencesNational Health and Medical Research CouncilNatural Sciences and Engineering Research Council of Canada
Keywords
FOXO1Protein kinase BEndocrinologyInternal medicineInsulinInsulin receptorCoactivatorBiologySkeletal muscleAKT2PhosphorylationMyogenesisAKT1Insulin resistanceTranscription factorCell biologyMedicineBiochemistryGene
Has abstract in OpenAlex
yes