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Salmonella ubiquitination: ARIH1 enters the fray
Author(s) -
LobatoMárquez Damián,
Mostowy Serge
Publication year - 2017
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.15252/embr.201744672
Subject(s) - bacteriology , salmonella , research centre , biology , library science , genetics , bacteria , computer science
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][Polajnar M, 2017] discover that Ring‐between‐Ring ( RBR ) E3 ligase ARIH 1 (also known as HHARI ) is involved in formation of the ubiquitin coat surrounding cytosolic Salmonella . Evidence suggests that ARIH 1, in cooperation with E3 ligases LRSAM 1 and HOIP , modulates the recognition of intracellular bacteria for cell‐autonomous immunity.