GSK3β-dependent phosphorylation of peroxisome proliferator-activated receptor-γ co-activator 1α (PGC-1α) in reponse to stress

<p><b>Copyright information:</b></p><p>Taken from "Dynamic regulation of PGC-1α localization and turnover implicates mitochondrial adaptation in calorie restriction and the stress response"</p><p></p><p>Aging Cell 2008;7(1):101-111.</p><p>Published online Jan 2008</p><p>PMCID:PMC2253697.</p><p>© 2008 The Authors Journal compilation © Blackwell Publishing Ltd/Anatomical Society of Great Britain and Ireland 2008</p> (A) Immunofluorescent detection of PGC-1α in cells 24 h following siRNA with negative control or GSK3β-specific oligonucleotides. Knock down of GSK3β detected by Western blot (lower panel). (B) Western blot detection of PGC-1α in extracts taken at the indicated times in minutes following hydrogen peroxide treatment (350 µ); cells were grown under normal conditions or in the presence of GSK3β inhibitor VII (20 µ) prior to and during stress. (C) Detection of PGC-1α by Western blot of GSK3β immunoprecipitates from untreated or hydrogen-peroxide-treated cells (350 µ, 15 min); cells were grown in the absence or presence of GSK3β inhibitor VII (20 µ). (D) Detection of PGC-1α in phosphoserine and phosphothreonine immunoprecipitates from hydrogen-peroxide-treated cells (350 µ, 15 min); cells were grown in the absence or presence of GSK3β inhibitor VII (20 µ). (E) Detection of phosphoserine and phosphothreonine phosphorylated species by Western blot of PGC-1α immunoprecipitates from hydrogen-peroxide-treated cells (350 µ, 15 min); cells were grown in the absence or presence of GSK3β inhibitor VII (20 µ). (F) Model of PGC-1α activation in response to oxidative stress