Identifying USPs regulating immune signals in Drosophila: USP2 deubiquitinates Imd and promotes its degradation by interacting with the proteasome.

ABSTRACT:

Background

Rapid activation of innate immune defences upon microbial infection depends on the evolutionary conserved NF-κB dependent signals which deregulation is frequently associated with chronic inflammation and oncogenesis. These signals are tightly regulated by the linkage of different kinds of ubiquitin moieties on proteins that modify either their activity or their stability. To investigate how ubiquitin specific proteases (USPs) orchestrate immune signal regulation, we created and screened a focused RNA interference library on Drosophila NF-κB-like pathways Toll and Imd in cultured S2 cells, and further analysed the function of selected genes in vivo.

Results

We report here that USP2 and USP34/Puf, in addition to the previously described USP36/Scny, prevent inappropr

SUBMITTER: Engel E 

PROVIDER: S-EPMC4140012 | biostudies-literature | 2014 Jul

REPOSITORIES: biostudies-literature