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An editable high resolution scientific image depicting Pyruvate Dehydrogenase Complex Regulation

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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