EspL is a bacterial cysteine protease effector that cleaves RHIM proteins to block necroptosis and inflammation.

ABSTRACT: Cell death signalling pathways contribute to tissue homeostasis and provide innate protection from infection. Adaptor proteins such as receptor-interacting serine/threonine-protein kinase 1 (RIPK1), receptor-interacting serine/threonine-protein kinase 3 (RIPK3), TIR-domain-containing adapter-inducing interferon-β (TRIF) and Z-DNA-binding protein 1 (ZBP1)/DNA-dependent activator of IFN-regulatory factors (DAI) that contain receptor-interacting protein (RIP) homotypic interaction motifs (RHIM) play a key role in cell death and inflammatory signalling^1-3. RHIM-dependent interactions help drive a caspase-independent form of cell death termed necroptosis^4,5. Here, we report that the bacterial pathogen enteropathogenic Escherichia coli (EPEC) uses the type III secretion sys

SUBMITTER: Pearson JS 

PROVIDER: S-EPMC7613272 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature