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demonstrate that the increased PDK3 activity in patient fibroblasts (PDK3(R158H)) leads to the attenuation of PDC (Montrer PDC Protéines) through hyper-phosphorylation of E1 at selected serine residues
The pyruvate dehydrogenase (Montrer PDP Protéines) kinases (PDKs) PDK1 (Montrer PDK1 Protéines) and PDK3 are direct targets of KDM4A (Montrer KDM4A Protéines) and E2F1 (Montrer E2F1 Protéines) and modulate the switch between glycolytic metabolism and mitochondrial oxidation.
We have identified a p.R158H PDK3 mutation in a Korean X-linked dominant Charcot-Marie-Tooth type 6 family
Accordingly, elevated levels of PDK1, PDK3, and PKM2 and reduced PK activity could be observed in iPSCs and human embryonic stem cells in the undifferentiated state
Reduced pyruvate flux due to R158H mutant PDK3-mediated hyper-phosphorylation of the pyruvate dehydrogenase (Montrer PDP Protéines) complex is the underlying pathogenic cause of peripheral neuropathy in X-linked dominant Charcot-Marie-Tooth disease.
Findings suggest the HIF-1 (Montrer HIF1A Protéines)/PDK3 bioenergetic pathway as a new target for therapeutic intervention in metastatic melanoma.
analysis of residues in L2 and residues in the C-terminal region and the lipoyl-binding pocket of PDK3 which are critical determinants for the cross-talk between L2 and PDK3, which up-regulates PDK3 activity
PDK2 (Montrer PDK2 Protéines), PDK3 and PDK4 (Montrer PDK4 Protéines) are primary PPARbeta (Montrer PPARD Protéines)/delta target genes in humans underlining the importance of the receptor in the control of metabolism
Distinct structural mechanisms for inhibition of PDK3 by AZD7545, dichloroacetate, and radicol.
increased PDK3 expression due to elevated HIF-1alpha (Montrer HIF1A Protéines) in cancer cells may play critical roles in metabolic switch during cancer progression and chemoresistance in cancer therapy
The pyruvate dehydrogenase (PDH) complex is a nuclear-encoded mitochondrial multienzyme complex that catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It provides the primary link between glycolysis and the tricarboxylic acid (TCA) cycle, and thus is one of the major enzymes responsible for the regulation of glucose metabolism. The enzymatic activity of PDH is regulated by a phosphorylation/dephosphorylation cycle, and phosphorylation results in inactivation of PDH. The protein encoded by this gene is one of the three pyruvate dehydrogenase kinases that inhibits the PDH complex by phosphorylation of the E1 alpha subunit. This gene is predominantly expressed in the heart and skeletal muscles. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
pyruvate dehydrogenase kinase, isozyme 3
, pyruvate dehydrogenase kinase, isoenzyme 3
, pyruvate dehydrogenase kinase 3
, pyruvate dehydrogenase [lipoamide] kinase isozyme 3, mitochondrial-like
, [Pyruvate dehydrogenase [lipoamide]] kinase isozyme 3, mitochondrial
, pyruvate dehydrogenase, lipoamide, kinase isozyme 3, mitochondrial
, Pyruvate dehydrogenase kinase 3