SUMOylation modulates eIF5A activities in both yeast and pancreatic ductal adenocarcinoma cells.

ABSTRACT:

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). Mutants were engineered by site-directed mutagenesis. Protein stability was measured by a cycloheximide chase

SUBMITTER: Seoane R 

PROVIDER: S-EPMC10790418 | biostudies-literature | 2024 Jan

REPOSITORIES: biostudies-literature