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AKT1 — PPARGC1A

Text-mined interactions from Literome

Oliveira et al., Am J Physiol Endocrinol Metab 2004 : Reduction of PGC-1alpha expression resulted in no modification of insulin induced tyrosine phosphorylation of the IR and Ser473 phosphorylation of Akt
Southgate et al., FASEB J 2005 (Insulin Resistance) : PGC-1alpha gene expression is down-regulated by Akt- mediated phosphorylation and nuclear exclusion of FoxO1 in insulin stimulated skeletal muscle
Bartke et al., Hormones (Athens) 2008 : Results obtained to date suggest that reduced Akt phosphorylation and PPAR beta/delta expression in the liver, reduced JNK1 phosphorylation and increased PGC1alpha expression in the muscle, and increased expression of IGF1 and insulin receptor in the heart are either related to mechanisms of CR action on longevity or represent potential biomarkers of delayed aging
Roman et al., Mol Cell Endocrinol 2010 : Central leptin action improves skeletal muscle AKT , AMPK, and PGC1 alpha activation by hypothalamic PI3K dependent mechanism
Xiong et al., J Biol Chem 2010 (Cardiovascular Diseases...) : We show that Ang II stimulates Akt dependent PGC-1 alpha serine 570 phosphorylation, which is required for the binding of the histone acetyltransferase GCN5 ( general control nonderepressible 5 ) to PGC-1 alpha and for its lysine acetylation