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Article

Gain-of-function R225W mutation in human AMPKgamma(3) causing increased glycogen and decreased triglyceride in skeletal muscle.

PloS one - 19 Sept 2007

Costford Sheila R, Kavaslar Nihan, Ahituv Nadav, Chaudhry Shehla N, Schackwitz Wendy S, Dent Robert, Pennacchio Len A, McPherson Ruth, Harper Mary-Ellen

Abstract excerpt

BACKGROUND: AMP-activated protein kinase (AMPK) is a heterotrimeric enzyme that is evolutionarily conserved from yeast to mammals and functions to maintain cellular and whole body energy homeostasis. Studies in experimental animals demonstrate that activation of AMPK in skeletal muscle protects against insulin resistance, type 2 diabetes and obesity. The regulatory gamma(3) subunit of AMPK is expressed...

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Source

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Identifiers

PMID: 17878938
DOI: 10.1371/journal.pone.0000903
PMCID: PMC1964808

Genes

PRKAG3

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Click a neighbor to travelStep 1 · 12 closest

Gain-of-function R225W mutation in human AMPKgamma(3) causing increased glycogen and decreased triglyceride in skeletal muscle.PMID 17878938Read ↗

Naturally occurring R225W mutation of the gene encoding AMP-activated protein kinase (AMPK)gamma(3) results in increased oxidative capacity and glucose uptake in human primary myotubes.Semantic proximity Read ↗

A mutation in PRKAG3 associated with excess glycogen content in pig skeletal muscle.Semantic proximity Read ↗

Metabolic functions of AMPK: aspects of structure and of natural mutations in the regulatory gamma subunits.Semantic proximity Read ↗

The human AMPKγ3 R225W mutation does neither enhance basal AMPKγ3-associated activity nor glycogen in human or mouse skeletal muscleSemantic proximity Read ↗

Opposite transcriptional regulation in skeletal muscle of AMP-activated protein kinase gamma3 R225Q transgenic versus knock-out mice.Semantic proximity Read ↗

Muscle-specific overexpression of wild type and R225Q mutant AMP-activated protein kinase gamma3-subunit differentially regulates glycogen accumulation.Semantic proximity Read ↗

Cloning and characterization of mouse 5'-AMP-activated protein kinase gamma3 subunit.Semantic proximity Read ↗

The human AMPKγ3 R225W mutation negatively impacts site-1 nucleotide binding and does not enhance basal AMPKγ3-associated activity nor glycogen production in human or mouse skeletal muscle.Semantic proximity Read ↗

Identification and characterization of AMPK gamma 3 mutations in the pig.Semantic proximity Read ↗

Human γ2-AMPK Mutations.Semantic proximity Read ↗

Role of AMP-activated protein kinase gamma 3 genetic variability in glucose and lipid metabolism in non-diabetic whites.Semantic proximity Read ↗

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