Atg8 is involved in endosomal and phagosomal acidification in the parasitic protist Entamoeba histolytica.

Autophagy is one of two major bulk protein degradation systems and is conserved throughout eukaryotes. The protozoan Entamoeba histolytica, which is a human intestinal parasite, possesses a restricted set of autophagy-related (Atg) proteins compared with other eukaryotes and thus represents a suitable model organism for studying the minimal essential components and ancestral functions of autophagy. E.

Analysis of autophagy in the enteric protozoan parasite Entamoeba.

Entamoeba histolytica is the enteric protozoan parasite that causes human amoebiasis. We have previously shown that autophagy is involved in proliferation and differentiation in the related species Entamoeba invadens, which infects reptiles and develops similar clinical manifestations. Because this group of protists possesses only a limited set of genes known to participate in autophagy in other eukaryotes, it potentially represents a useful model for studying the core system of autophagy and provides tools to elucidate the evolution of eukaryotes and their organelles.

Autophagy during proliferation and encystation in the protozoan parasite Entamoeba invadens.

Autophagy is one of the three systems responsible for the degradation of cytosolic proteins and organelles. Autophagy has been implicated in the stress response to starvation, antigen cross-presentation, the defense against invading bacteria and viruses, differentiation, and development. Saccharomyces cerevisiae Atg8 and its mammalian ortholog, LC3, play an essential role in autophagy.

Entamoeba histolytica: identification of EhGPCR-1, a novel putative G protein-coupled receptor that binds to EhRabB.

EhRabB is an Entamoeba histolytica protein involved in phagocytosis. However, proteins that regulate the EhRabB activity are unknown. Here, we report the identification of a putative G protein-coupled receptor of E.