Dimitri Vanauberg

All Publications

• Mammalian fatty acid synthase and<i> O</i>-GlcNAc transferase preferentially interact<i> via</i> their respective<i> N</i>-terminal regions BIOCHEMISTRY AND BIOPHYSICS REPORTS Vanauberg, D., Brysbaert, G., Raouraoua, N., Mistarz-Gruau, P., Lensink, M. F., Vercoutter-Edouart, A., Lefebvre, T. 2026; 45: 102427

  Abstract

  Fatty Acid Synthase (FASN) is a central enzyme in the de novo lipogenesis pathway. By producing fatty acids, FASN is implicated in numerous crucial cellular processes, but it is also frequently overexpressed in cancer. O-GlcNAc Transferase (OGT) governs the addition of N-acetylglucosamine residues onto cytosolic, nuclear and mitochondrial proteins. Like FASN, OGT actively participates in carcinogenesis. We previously showed that OGT regulates FASN in different ex vivo and in vivo models. Reciprocally, FASN promotes OGT expression and activity. The two enzymes physically interact together and contribute to cancer cell survival. It is therefore fundamental to define the respective interaction region of each enzyme to explore new therapeutic solutions for patients suffering from cancer. By using the hepatocarcinoma cell line Hep3B, we show thanks to two series of deletion mutants that both enzymes preferentially interact via their respective N-terminal regions. Analysis of the O-GlcNAc status of the various FASN deletion mutants shows that stronger interaction with OGT correlates with higher glycosylation, suggesting that OGT catalyzes the transfer of GlcNAc with limited substrate specificity.

  View details for DOI 10.1016/j.bbrep.2025.102427

  View details for Web of Science ID 001662881100007

  View details for PubMedID 41550490

  View details for PubMedCentralID PMC12808501