EhVps35, a retromer component, is a key factor in secretion, motility, and tissue invasion by Entamoeba histolytica.

ABSTRACT: In humans and Drosophila melanogaster, the functional convergence of the endosomal sorting complex required for transport (ESCRT) machinery that is in charge of selecting ubiquitinated proteins for sorting into multivesicular bodies, and the retromer, that is the complex responsible for protein recycling to the plasma membrane and Golgi apparatus. ESCRT and retromer complexes are codependent for protein sorting recycling, degradation, and secretion. In this article, we studied the EhVps35 C isoform (referred to as EhVps35), that is the central member of the Entamoeba histolytica retromer, and its relation with the ESCRT machinery during sorting and protein recycling events and their involvement virulence. Our findings revealed that EhVps35 interacts with at least 300 proteins

SUBMITTER: Diaz-Valdez J 

PROVIDER: S-EPMC11466944 | biostudies-literature | 2024

REPOSITORIES: biostudies-literature