Bacterial E3 ligase effectors exploit host ubiquitin systems
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Updated: Mar 11, 2026

In-vitro Reconstitution of Bacterial Ubiquitination and VCP/p97-mediated Elimination
Published on: January 2, 2026
Hiroshi Ashida1, Chihiro Sasakawa2
1Division of Bacterial Infection Immunology, Medical Mycology Research Center, Chiba University, 1-8-1 Inohana, Chuo-ku, Chiba, Japan.
Abstract:
Ubiquitination is a crucial post-translational protein modification involved in regulation of various cellular processes in eukaryotes. In particular, ubiquitination is involved in multiple aspects of bacterial infection and host defense mechanisms. In parallel with the identification of ubiquitination as a component of host defense systems, recently accumulated evidence shows that many bacterial pathogens exploit host ubiquitin systems to achieve successful infection. Here, we highlight the strategies by which bacteria subvert host ubiquitin systems by mimicking E3 ubiquitin ligase activity.
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