Legionella pneumophila balances ubiquitin transglutamination
- 28 January 2020
- journal article
- editorial
- Published by EMBO in The EMBO Journal
- Vol. 39 (4), e104258
- https://doi.org/10.15252/embj.2019104258
Abstract
The effector MavC of the bacterial pathogen Legionella pneumophila catalyzes a noncanonical ubiquitination of the host ubiquitin‐conjugating E2 enzyme UBE2N by crosslinking a glutamine residue of ubiquitin to UBE2N lysine residues via its transglutaminase activity. A new study by Gan et al (2020) reveals that L. pneumophila reverses this noncanonical ubiquitination via its ubiquitin deamidase effector MvcA to allow precise temporal regulation of host signaling during infection.This publication has 11 references indexed in Scilit:
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