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Article

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

The Journal of biological chemistry - 17 Mar 2006

Nilsson Elisabeth C, Long Yun Chau, Martinsson Sofia, Glund Stephan, Garcia-Roves Pablo, Svensson L Thomas, Andersson Leif, Zierath Juleen R, Mahlapuu Margit

Abstract excerpt

AMP-activated protein kinase (AMPK) is an evolutionarily conserved heterotrimer important for metabolic sensing in all eukaryotes. The muscle-specific isoform of the regulatory gamma-subunit of the kinase, AMPK gamma3, has an important role in glucose uptake, glycogen synthesis, and fat oxidation in white skeletal muscle, as previously demonstrated by physiological characterization of AMPK gamma3 mutant (R225Q)...

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PMID: 16410251
DOI: 10.1074/jbc.M510461200

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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.

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Opposite transcriptional regulation in skeletal muscle of AMP-activated protein kinase gamma3 R225Q transgenic versus knock-out mice.PMID 16410251Read ↗

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

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

Role of AMP--activated protein kinase in the control of glucose homeostasis.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 ↗

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

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 ↗

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 ↗

5'-AMP-activated protein kinase regulates skeletal muscle glycogen content and ergogenics.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 ↗

Characterization of the role of gamma2 R531G mutation in AMP-activated protein kinase in cardiac hypertrophy and Wolff-Parkinson-White syndrome.Semantic proximity Read ↗

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