A common enzyme takes on a surprising role in preventing cancer

 

Originally published by Justin Jackson, Phys.org, on May 19, 2025

Edited by Sadie Harley, reviewed by Robert Egan

Working model revealing the role of ALDH4A1 in maintaining an active MPC complex for mitochondrial pyruvate import and TCA cycle entry. Credit: Nature Cell Biology (2025). DOI: 10.1038/s41556-025-01651-8

Researchers at Duke University Medical Center and Wake Forest University School of Medicine have identified ALDH4A1, a mitochondrial proline-metabolizing enzyme, as a third structural component of the mitochondrial pyruvate carrier (MPC) complex. Forming a trimeric assembly with MPC1 and MPC2, ALDH4A1 maintains MPC integrity and facilitates pyruvate import into mitochondria.

Mitochondrial pyruvate import serves as a critical step in cellular energy metabolism, linking cytosolic glycolysis to mitochondrial oxidative phosphorylation. Disruptions in this pathway can promote cancer cell proliferation by increasing cytosolic pyruvate and driving glycolytic metabolism, a phenomenon often associated with the Warburg effect.

Understanding how the MPC complex regulates pyruvate import may reveal metabolic vulnerabilities in cancer.

MPC1 and MPC2, the core subunits of the mitochondrial pyruvate carrier complex, serve as the conduit for pyruvate entry into mitochondria. Identification of additional regulatory components had not been observed until now.

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