Protein ubiquitination is a posttranslational modification that regulates many aspects of cellular life, including proteostasis, vesicular trafficking, DNA repair and NF-κB activation. By directly targeting intracellular bacteria or bacteria-containing vacuoles to the lysosome, ubiquitination is also an important component of cell-autonomous immunity. Not surprisingly, several pathogenic bacteria encode deubiquitinases (DUBs) and use them as secreted effectors that prevent ubiquitination of bacterial components. A systematic overview of known bacterial DUBs, including their cleavage specificities and biological roles, suggests multiple independent acquisition events from host-encoded DUBs and other proteases. The widely used classification of DUBs into seven well-defined families should only be applied to eukaryotic DUBs, since several bacterial DUBs do not follow this classification.
-
Cover Image
Cover Image
The second messenger 3′,5′-cyclic nucleoside adenosine monophosphate (cAMP) plays a key role in signal transduction across prokaryotes and eukaryotes. In this issue Klausen and colleagues (1733–1748) provide an overview about the optogenetic tools and biosensors used to explore the subcellular organization of cAMP signalling. The cover image depicts time projection (colour represents time) of a head-tethered transgenic mouse sperm expressing the photo-activated adenylate cyclase bPAC. Image courtesy of Dagmar Wachten.
Bacterial DUBs: deubiquitination beyond the seven classes
Thomas Hermanns, Kay Hofmann; Bacterial DUBs: deubiquitination beyond the seven classes. Biochem Soc Trans 20 December 2019; 47 (6): 1857–1866. doi: https://doi.org/10.1042/BST20190526
Download citation file:
Sign in
Sign in to your personal account
Biochemical Society Member Sign in
Sign InSign in via your Institution
Sign in via your InstitutionGet Access To This Article
Get Email Alerts
Open Access for all
We offer compliant routes for all authors from 2025. With library support, there will be no author nor reader charges in 5 journals. Check here |
![]() |