Rocío Seoane, Tomás Lama-Díaz, Antonia María Romero, Ahmed El Motiam, Arantxa Martínez-Férriz, Santiago Vidal, Yanis H Bouzaher, María Blanquer, Rocío M Tolosa, Juan Castillo Mewa, Manuel S Rodríguez, Adolfo García-Sastre, Dimitris Xirodimas, James D Sutherland, Rosa Barrio, Paula Alepuz, Miguel G Blanco, Rosa Farràs, Carmen Rivas
BACKGROUND: The eukaryotic translation initiation protein eIF5A is a highly conserved and essential factor that plays a critical role in different physiological and pathological processes including stress response and cancer. Different proteomic studies suggest that eIF5A may be a small ubiquitin-like modifier (SUMO) substrate, but whether eIF5A is indeed SUMOylated and how relevant is this modification for eIF5A activities are still unknown. METHODS: SUMOylation was evaluated using in vitro SUMOylation assays, Histidine-tagged proteins purification from His6-SUMO2 transfected cells, and isolation of endogenously SUMOylated proteins using SUMO-binding entities (SUBES)...
January 16, 2024: Cellular & Molecular Biology Letters