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© Research
Publication : Cellular Microbiology

Acetylation is the most abundant actin modification in Entamoeba histolytica and modifications of actin’s amino-terminal domain change cytoskeleton activities

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Cellular Microbiology - 10 Apr 2019

Hernández-Cuevas NA, Jhingan GD, Petropolis D, Vargas M, Guillen N

Link to Pubmed [PMID] – 30506797

Link to DOI – 10.1111/cmi.12983.

Cell Microbiol. 2019 Apr;21(4):e12983

Actin is one of the most conserved, abundant, and ubiquitous proteins in all eukaryotes characterised to date. Posttranslation modifications of actin modify the organisation of the actin-rich cytoskeleton. In particular, chemical modifications of actin’s amino-terminal region determine how filamentous actin is organised into scaffolds. After assuming that protein modifications account for the multiple functional activities exerted by the single actin in Entamoeba histolytica, we profiled posttranslational modifications of this protein. Acetylation (on 21 different amino acids) was the most abundant modification, followed by phosphorylation. Furthermore, the glycine residue at Position 2 in E. histolytica’s actin (Gly2, not found in most other eukaryotic actins) was found to be acetylated. The impact of Gly2 on the amoeba’s life cycle and pathogenicity was then assessed in mutagenesis experiments. We found that Gly2 was necessary for cell morphology and division, parasite-host cell adhesion, and host invasion in an in vitro model of amoebic human infection.