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Salmonella ubiquitination: ARIH1 enters the fray

Ubiquitination is a post‐translational modification in which ubiquitin, a 76‐amino acid polypeptide, is covalently bound to one or more lysines of a target protein. Ubiquitination is mediated by the coordinated activity of ubiquitin activating (E1), conjugating (E2), and ligating (E3) enzymes. Ubiqu...

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Detalles Bibliográficos
Autores principales: Lobato‐Márquez, Damián, Mostowy, Serge
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5579349/
https://www.ncbi.nlm.nih.gov/pubmed/28821533
http://dx.doi.org/10.15252/embr.201744672
Descripción
Sumario:Ubiquitination is a post‐translational modification in which ubiquitin, a 76‐amino acid polypeptide, is covalently bound to one or more lysines of a target protein. Ubiquitination is mediated by the coordinated activity of ubiquitin activating (E1), conjugating (E2), and ligating (E3) enzymes. Ubiquitin is widely investigated for its ability to regulate key biological processes in the cell, including protein degradation and host–bacteria interactions. The determinants underlying bacterial ubiquitination, and their precise roles in host defense, have not been fully resolved. In this issue of EMBO Reports, Polajnar et al 1 discover that Ring‐between‐Ring (RBR) E3 ligase ARIH1 (also known as HHARI) is involved in formation of the ubiquitin coat surrounding cytosolic Salmonella. Evidence suggests that ARIH1, in cooperation with E3 ligases LRSAM1 and HOIP, modulates the recognition of intracellular bacteria for cell‐autonomous immunity.