Protein Sumoylation Is Crucial for Phagocytosis in Entamoeba histolytica Trophozoites.

ABSTRACT: Posttranslational modifications provide Entamoeba histolytica proteins the timing and signaling to intervene during different processes, such as phagocytosis. However, SUMOylation has not been studied in E. histolytica yet. Here, we characterized the E. histolytica SUMO gene, its product (EhSUMO), and the relevance of SUMOylation in phagocytosis. Our results indicated that EhSUMO has an extended N-terminus that differentiates SUMO from ubiquitin. It also presents the GG residues at the C-terminus and the ΨKXE/D binding motif, both involved in target protein contact. Additionally, the E. histolytica genome possesses the enzymes belonging to the SUMOylation-deSUMOylation machinery. Confocal microscopy assays disclosed a remarkable EhSUMO membrane activity with con

SUBMITTER: Diaz-Hernandez M 

PROVIDER: S-EPMC8198320 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature