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Cell Microbiol. 2019 Apr;21(4):e12983. doi: 10.1111/cmi.12983. Epub 2018 Dec 21.

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

Author information

1
Institut Pasteur, Unité Biologie Cellulaire du Parasitisme, Paris, France.
2
INSERM Unit 786, Paris, France.
3
National Institute of Immunology, New Delhi, India.
4
Departamento de Biomedicina Molecular, Instituto Politécnico Nacional, Centro de Investigación y de Estudios Avanzados CINVESTAV, Mexico City, Mexico.
5
Centre National de la Recherche Scientifique, ERL9195, Paris, France.

Abstract

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.

PMID:
30506797
DOI:
10.1111/cmi.12983

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