UFMylation of Pyruvate Dehydrogenase Regulates Mitochondrial Metabolism
Posted on: 20 April 2026
Preprint posted on 18 March 2026
UFMylation, discovered for the first time in mitochondrial proteins, is found to keep pyruvate dehydrogenase activity and downstream glucose oxidation in check.
Selected by Hannah Pletcher
Categories: biochemistry, cell biology
Figure caption: Model proposed by the preprint authors in which UFSP2 regulates PDH activity through DLAT UFMylation. In UFSP2 deficient cells, DLAT is highly UFMylated, increasing PDH activity and downstream TCA cycle activity and oxidative phosphorylation. Figure 5G from Nguyen & Wu et al., 2026 on bioRxiv; preprint is available under a CC-BY 4.0 International license.
Background:
Discovered roughly twenty years ago, UFMylation is a ubiquitin-like post-translational modification (PTM). Sharing a similar fold and conjugation system to ubiquitin, Ubiquitin-Fold Modifier 1 (UFM1) is attached to lysine residues. When dysregulated, this PTM has been implicated in disease, like developmental disorders, neurodegeneration, and cancer. UFMylation is emerging as an important regulator of processes like ribosome-associated quality control and endoplasmic reticulum-associated stress responses (Komatsu et al., 2026). However, much of the functional characterization of UFMylation has focused on the conjugation of UFM1, while the consequence of UFM1 removal from proteins by UFMylase UFSP2 is unclear.
In this preprint, the authors sought to elucidate the function of UFSP2. In UFSP2 knockout (KO) cells, the scientists discovered a buildup of mitochondrial UFMylated proteins, including a UFMylated subunit of the pyruvate dehydrogenase complex (PDH) that results in increased PDH activity and downstream glucose oxidation (Nguyen & Wu et al., 2026).
What I liked/why this new work is important:
This preprint helps to define the function of UFMylase UFSP2, uncovers a novel role for UFMylation in the mitochondria, and identifies how a particular UFMylation site on dihydrolipoamide S-acetyltransferase (DLAT) can regulate glucose metabolism through PDH activity. In addition to understanding how UFMylation regulates cells on a basic level, the authors speculated on how their findings could contribute to the pathophysiology of UFSP2-associated diseases. I really enjoyed reading how the authors employed a large discovery-based screen, observed an interesting cellular phenotype, and used a combination of mass spectrometry, isotope labeling, and enzyme assays to identify a specific UFMylation site regulating this phenotype. The work is elegant, rigorous, and digestible.
Key findings:
UFSP2 KO results in UFMylated mitochondrial proteins and increased mitochondrial function.
The authors conducted immunoprecipitation-coupled mass spectrometry on UFSP2 KO 293T cells overexpressing the UFMylation conjugation system to search for candidate UFMylated proteins. They validated their method by identifying known UFMylated targets in addition to many new UFMylated candidates. Approximately 15% of enriched UFMylated proteins were mitochondrial proteins. Further, UFSP2 KO cell lines showed an increased oxygen consumption rate and canonical TCA cycle activity by glucose labeling. These data suggest a novel role for UFMylation in regulating mitochondrial function and specifically glucose oxidation.
DLAT, a subunit of PDH, is UFMylated in UFSP2 KO cells, causing increased PDH activity.
Using stable isotope tracing, the authors found that the increase in glucose oxidation originates upstream of the TCA cycle at the PDH step. PDH converts pyruvate to acetyl-CoA to enter the TCA cycle. Stable isotope tracing and an immunoprecipitation-based activity assay showed increased PDH activity in UFSP2 KO cells and UFSP2 KO cells rescued with catalytically inactive UFSP2. The authors discovered that DLAT, a PDH subunit, is UFMylated at lysine residue 118, causing the increased PDH activity. They validated these findings by rescuing UFSP2/DLAT double KO cells with DLAT K118R to disrupt UFMylation, resulting in decreased oxygen consumption rate and acetyl-CoA labeling from stable isotope tracing compared to WT DLAT rescue.
Future directions & questions for the authors:
- In the Discussion, you proposed a model for how DLAT UFMylation increases PDH activity. Do you plan to investigate this model in future experiments? What do you think would be the best way to test this model?
- I found it interesting that mitoribosome proteins were found to be UFMylation targets. Can you speculate on how UFMylation could regulate the mitoribosome? Do you think mitoribosome UFMylation has any similarities to UFMylation of ribosomal proteins? Is this an area you plan to pursue in the future?
- Is it known how UFSP2 can localize to different organelles? Is this localization regulated or expected to change in different cellular contexts?
References:
Komatsu, M., Noda, N. N., & Inada, T. (2026). The mechanistic basis and cellular functions of UFMylation. Nature Reviews Molecular Cell Biology. https://doi.org/10.1038/s41580-025-00944-y.
Nguyen, P. T., Wu, Z., Kim, D., Ogu, T., Yin, S., Sondhi, V., Cai, F., Tippetts, T. S., Jen, A., Shishkova, E., Cai, L., Dumesnil, D., Cervantes, M., Chen, H., Mishra, P., Coon, J. J., Hoxhaj, G., Ni, M., & DeBerardinis, R. J. (2026). UFMylation of Pyruvate Dehydrogenase Regulates Mitochondrial Metabolism. BioRxiv: The Preprint Server for Biology, 2026.03.18.712693. https://doi.org/10.64898/2026.03.18.712693.
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