Clking on PGC-1alpha to inhibit gluconeogenesis.
The link between Akt activation and gluconeogenic repression remains unclear, despite many years of investigation and remarkable progress. Rodgers and colleagues now introduce us to the Clk2 kinase, an Akt substrate that can directly phosphorylate and inhibit PGC-1alpha, blunting hepatic glucose production.
Cantó
Carles
C
Ecole Polytechnique Fédérale de Lausanne, Switzerland.
Auwerx
Johan
J
D000107:Acetylation; D005943:Gluconeogenesis; D006360:Heat-Shock Proteins / Q000378:metabolism*; D006801:Humans; D007328:Insulin / Q000378:metabolism; D000071248:Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism; D011505:Protein-Tyrosine Kinases / Q000378:metabolism; D051057:Proto-Oncogene Proteins c-akt / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism*
D006360:Heat-Shock Proteins; D007328:Insulin; C486497:PPARGC1A protein, human; D000071248:Peroxisome Proliferator-Activated Receptor Gamma Coactivator 1-alpha; D014157:Transcription Factors; C066780:Clk dual-specificity kinases; D011505:Protein-Tyrosine Kinases; D017346:Protein Serine-Threonine Kinases; D051057:Proto-Oncogene Proteins c-akt