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Pyruvate dehydrogenase kinase, isozyme 3

PDK3, pyruvate dehydrogenase kinase 3
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. [provided by RefSeq, Mar 2010] (from NCBI)
Top mentioned proteins: PDK1, PDK4, PDK2, Insulin, ACID
Papers on PDK3
Novel molecular mechanisms involved in hormonal regulation of lactate production in Sertoli cells.
Riera et al., Buenos Aires, Argentina. In Reproduction, Oct 2015
As for the regulation of PDC, analysis of pyruvate dehydrogenase kinase (Pdk) expression showed that FSH increases Pdk3 and decreases Pdk4 mRNA levels while bFGF increases the expression of all Pdks.
Differing roles of pyruvate dehydrogenase kinases during mouse oocyte maturation.
Wang et al., Nanjing, China. In J Cell Sci, Aug 2015
We found that PDK3-mediated phosphorylation of Ser293-PDHE1α results in disruption of meiotic spindle morphology and chromosome alignment and decreased total ATP levels, probably through inhibition of PDH activity.
Recent advances in Charcot-Marie-Tooth disease.
Timmerman et al., Antwerp, Belgium. In Curr Opin Neurol, 2014
RECENT FINDINGS: Several new Charcot-Marie-Tooth disease-causing genes have been recently identified, further enlarging the genetic diversity and phenotypic variability, including: SBF1, DHTKD1, TFG, MARS, HARS, HINT1, TRIM1, AIFM1, PDK3 and GNB4.
HIF1α modulates cell fate reprogramming through early glycolytic shift and upregulation of PDK1-3 and PKM2.
Adjaye et al., Berlin, Germany. In Stem Cells, 2014
Transcriptional and bioenergetic analysis during reprogramming initiation indicated that the transduction of the four factors is sufficient to upregulate the HIF1α target pyruvate dehydrogenase kinase (PDK) one and set in motion the glycolytic shift.
Role of the cytoskeleton in muscle transcriptional responses to altered use.
Lieber et al., San Diego, United States. In Physiol Genomics, 2013
The largest transcriptional changes were observed in the interaction between aging and the absence of desmin, including many genes related to slow fiber pathway (Myh7, Myl3, Atp2a2, and Casq2) and insulin sensitivity (Tlr4, Trib3, Pdk3, and Pdk4).
A new locus for X-linked dominant Charcot-Marie-Tooth disease (CMTX6) is caused by mutations in the pyruvate dehydrogenase kinase isoenzyme 3 (PDK3) gene.
Nicholson et al., Australia. In Hum Mol Genet, 2013
Whole exome sequencing identified a missense mutation c.G473A (p.R158H) in the pyruvate dehydrogenase kinase isoenzyme 3 (PDK3) gene.
Inactivation of the HIF-1α/PDK3 signaling axis drives melanoma toward mitochondrial oxidative metabolism and potentiates the therapeutic activity of pro-oxidants.
Marchetti et al., Lille, France. In Cancer Res, 2012
Pharmacologic or genetic blockades of the HIF-1α pathway decreased glycolysis and promoted mitochondrial respiration via specific reduction in the expression of pyruvate dehydrogenase kinase-3 (PDK3).
Pyruvate dehydrogenase E1α phosphorylation is induced by glucose but does not control metabolism-secretion coupling in INS-1E clonal β-cells.
Wiederkehr et al., Genève, Switzerland. In Biochim Biophys Acta, 2012
INS-1E cells and primary β-cells express pyruvate dehydrogenase kinase (PDK) 1, 2 and 3, which mediate the observed phosphorylation.
A novel Xp22.11 deletion causing a syndrome of craniosynostosis and periventricular nodular heterotopia.
Robertson et al., Dunedin, New Zealand. In Am J Med Genet A, 2011
Array comparative genomic hybridization has demonstrated a 300  kb interstitial deletion on Xp22.11 affecting all or part of three annotated genes, ZFX, PDK3, and PCYT1B in this subject.
Overexpression of pyruvate dehydrogenase kinase 3 increases drug resistance and early recurrence in colon cancer.
Tsai et al., Tainan City, Taiwan. In Am J Pathol, 2011
Pyruvate dehydrogenase kinase-1 (PDK1) and PDK3 participate in the metabolic switch of cancer cells; however, the medical significance of PDK1 and PDK3 in cancer progression is not known.
PDH activation during in vitro muscle contractions in PDH kinase 2 knockout mice: effect of PDH kinase 1 compensation.
Peters et al., Canada. In Am J Physiol Regul Integr Comp Physiol, 2011
PDH is deactivated by a set of PDH kinases (PDK1, PDK2, PDK3, PDK4), with PDK2 and PDK4 being the most predominant isoforms in skeletal muscle.
Induction of pyruvate dehydrogenase kinase-3 by hypoxia-inducible factor-1 promotes metabolic switch and drug resistance.
Tsai et al., Tainan City, Taiwan. In J Biol Chem, 2008
increased PDK3 expression due to elevated HIF-1alpha in cancer cells may play critical roles in metabolic switch during cancer progression and chemoresistance in cancer therapy
Three members of the human pyruvate dehydrogenase kinase gene family are direct targets of the peroxisome proliferator-activated receptor beta/delta.
Carlberg et al., Kuopio, Finland. In J Mol Biol, 2007
PDK2, PDK3 and PDK4 are primary PPARbeta/delta target genes in humans underlining the importance of the receptor in the control of metabolism
Distinct structural mechanisms for inhibition of pyruvate dehydrogenase kinase isoforms by AZD7545, dichloroacetate, and radicicol.
Chuang et al., Dallas, United States. In Structure, 2007
Distinct structural mechanisms for inhibition of PDK3 by AZD7545, dichloroacetate, and radicol.
Crystal structure of an asymmetric complex of pyruvate dehydrogenase kinase 3 with lipoyl domain 2 and its biological implications.
Vassylyev et al., Birmingham, United States. In J Mol Biol, 2007
crystal structure of the asymmetric PDHK3/lipoyl domain 2 complex; data suggest that the asymmetric complex represents a physiological state in which binding of a single L2-domain activates one of the PDHK protomers while inactivating another
Pyruvate dehydrogenase kinase regulatory mechanisms and inhibition in treating diabetes, heart ischemia, and cancer.
Hiromasa et al., Manhattan, United States. In Cell Mol Life Sci, 2007
The fraction of pyruvate dehydrogenase complex (PDC) in the active form is reduced by the activities of dedicated PD kinase isozymes (PDK1, PDK2, PDK3 and PDK4).
Structural determinants for cross-talk between pyruvate dehydrogenase kinase 3 and lipoyl domain 2 of the human pyruvate dehydrogenase complex.
Chuang et al., Dallas, United States. In J Biol Chem, 2006
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
Therapeutic potential of the mammalian pyruvate dehydrogenase kinases in the prevention of hyperglycaemia.
Holness et al., London, United Kingdom. In Curr Drug Targets Immune Endocr Metabol Disord, 2002
This review describes recent advances relating to the control of mammalian PDC activity by phosphorylation (inactivation) and dephosphorylation (activation, reactivation), in particular regulation of PDC by pyruvate dehydrogenase kinase (PDK) which phosphorylates and inactivates PDC.
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