title: Bacterial E3 ligase effectors exploit host ubiquitin systems.
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.
authors.affiliation: Division of Bacterial Infection Immunology, Medical Mycology Research Center, Chiba University, 1-8-1 Inohana, Chuo-ku, Chiba, Japan. Electronic address: hashida@chiba-u.jp.
authors.forename: Hiroshi
authors.initials: H
authors.lastname: Ashida
authors.affiliation: Nippon Institute for Biological Science, 9-2221-1 Shinmachi, Ome, 198-0024, Tokyo, Japan; Medical Mycology Research Center, Chiba University, 1-8-1 Inohana, Chuo-ku, 260-8673, Chiba, Japan.
authors.forename: Chihiro
authors.initials: C
authors.lastname: Sasakawa
mesh_terms: D001419:Bacteria / Q000201:enzymology* / Q000378:metabolism / Q000472:pathogenicity*; D001424:Bacterial Infections / Q000378:metabolism / Q000382:microbiology*; D054884:Host-Pathogen Interactions; D006801:Humans; D000069296:Type III Secretion Systems / Q000378:metabolism; D000069319:Type IV Secretion Systems / Q000378:metabolism; D044767:Ubiquitin-Protein Ligases / Q000235:genetics / Q000378:metabolism*; D054875:Ubiquitination; D037521:Virulence Factors / Q000378:metabolism
chemical_list: D000069296:Type III Secretion Systems; D000069319:Type IV Secretion Systems; D037521:Virulence Factors; D044767:Ubiquitin-Protein Ligases