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Stepihar, D.

Publications and source records attributed to Stepihar, D..

2 recordsLinked to original sources

Testis-Specific MAGEA3/6 Regulate Glycolysis to Promote Metabolic Flexibility and Reveal Therapeutic Vulnerabilities in Pancreatic Cancer Cells

Pancreatic ductal adenocarcinoma (PDAC) is an aggressive tumor characterized by metabolic plasticity that enables cancer cells to survive nutrient deprivation and therapeutic stress. Melanoma-associated antigens A3 and A6 (MAGEA3/6), members of the cancer-testis antigen family with a previously identified protective role in spermatogenesis during nutritional stress, have been implicated in cancer progression and metabolic regulation. However, their contribution to metabolic adaptation in pancreatic cancer remains poorly understood. Here, we investigated the molecular mechanisms underlying MAGEA3/6-mediated resistance to glycolytic inhibition using complementary gain- and loss-of-function models, pharmacological inhibition of metabolic pathways, cellular metabolic assays, and integrated transcriptomic, proteomic, metabolomic, and lipidomic analyses. MAGEA3/6 expression enhanced resistance to 2-deoxy-D-glucose (2-DG), with MAGEA6-expressing MIA PaCa-2 cells exhibiting a greater than 2.5-fold increase in the half-maximal inhibitory concentration (IC50). Conversely, MAGEA3/6 depletion reduced clonogenic growth and migration and increased sensitivity to 2-DG. Resistance persisted despite pharmacological inhibition of mTORC1, the pentose phosphate pathway, or glutaminase, suggesting metabolic adaptations beyond these pathways. Unexpectedly, MAGEA6 expression was associated with increased rather than decreased AMPK1 protein abundance, contrasting with previously reported MAGEA3/6-mediated AMPK degradation and suggesting context-dependent regulation of this master regulator of cellular metabolism. MAGEA6 also reduced hexokinase HK1 and HK2 abundance while increasing several downstream glycolytic enzymes, revealing discordant regulation of glycolysis. Seahorse analyses and integrated multi-omics profiling identified extensive remodeling of mitochondrial metabolism, glutamine-aspartate metabolism, phospholipid composition, lipid storage, and redox homeostasis. Interestingly, despite enhanced resistance to glycolytic inhibition, MAGEA6-expressing cells exhibited increased sensitivity to hydrogen peroxide-induced oxidative stress, revealing a potential metabolic vulnerability. Given that MAGEA3/6 are physiologically expressed primarily in the male germline during early spermatogenesis, a process highly sensitive to metabolic and oxidative stress, these findings also raise important questions about their physiological roles in protecting developing germ cells and maintaining metabolic and redox homeostasis. Together, our findings recognize MAGEA3/6 as regulators of metabolic plasticity in PDAC and highlight how understanding their molecular functions in both spermatogenesis and cancer may uncover previously unrecognized metabolic vulnerabilities and potential therapeutic opportunities.

cancer biology↗

Mechanisms of USP7/MAGEL2 Complex Assembly and Its Mutational Disruption in Neurodevelopmental Diseases

The WASH complex regulates endosomal trafficking and is linked to several neurodevelopmental diseases, including Prader-Willi syndrome, Schaaf-Yang syndrome, and Hao-Fountain syndrome. Its function is tightly controlled by ubiquitination, maintained by the multi-subunit MUST complex containing both a ubiquitin ligase (MAGEL2/TRIM27) and a deubiquitinase (USP7). However, the mechanism underlying the MUST complex assembly remains poorly understood. In this study, we investigate the assembly of USP7 and MAGEL2 components of the MUST complex using NMR spectroscopy, isothermal titration calorimetry, X-ray crystallography, and cellular assays. We show that the USP7/MAGEL2 interaction is bipartite and multivalent. Two distinct domains of USP7, TRAF and UBL1-2, recognize two unstructured but evolutionarily conserved regions of MAGEL2, one of which contains multiple TRAF-binding sites. Furthermore, we determine the high-resolution crystal structure of the TRAF/MAGEL2 complex and identify Hao-Fountain syndrome-linked mutations in USP7 that disrupt USP7/MAGEL2 complex formation in vitro and in cells. These findings provide mechanistic insight into the pathogenic basis of Hao-Fountain syndrome and related Schaaf-Yang and Prader-Willi syndromes.

biochemistry↗