Pyruvate Dehydrogenase Complex Regulation
Description
Pyruvate Dehydrogenase Complex (PDH) activity is regulated via phosphorylation and dephosphorylation, mediated by Pyruvate Dehydrogenase Kinase (PDK) and Pyruvate Dehydrogenase Phosphatase (PDP), respectively, in a cyclic manner in the mitochondrial matrix. Phosphorylation inhibits the PDH complex, whereas dephosphorylation activates it.
Acknowledgements
References
# Liang, Z., Ralph-Epps, T., Schmidtke, M. W., Kumar, V. & Greenberg, M. L. Decreased pyruvate dehydrogenase activity in Tafazzin-deficient cells is caused by dysregulation of pyruvate dehydrogenase phosphatase 1 (PDP1). J Biol Chem, 105697, doi:10.1016/j.jbc.2024.105697 (2024).
# Liang, Z., Ralph-Epps, T., Schmidtke, M. W., Lazcano, P., Denis, S. W., Balazova, M., Chakkour, M., Hazime, S., Ren, M., Schlame, M., Houtkooper, R. & Greenberg, M. Upregulation of the AMPK-FOXO1-PDK4 pathway is a primary mechanism of pyruvate dehydrogenase activity reduction and leads to
increased glucose uptake in tafazzin-deficient cells. bioRxiv, 2024.2002.2003.578755, doi:10.1101/2024.02.03.578755 (2024).
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