Work

Shutdown of interferon signaling by a viral-hijacked E3 ubiquitin ligase

Year: 2017

Type: article

Abstract: [2017; mBio 8(4): e01213-17], we describe molecular requirements that govern NSP1 recognition of β-TrCP, including an essential degron phosphorylation event, and the step-wise incorporation of NSP1 into hijacked cullin-RING E3 ligases (CRLs) that ubiquitinate and tag β-TrCP for degradation. Notably, although β-TrCP is chiefly recognized for its role as a master regulator of NF-κB signaling and IFN expression, β-TrCP also controls the stability of checkpoint proteins implicated in numerous other cellular pathways with antiviral activities, including autophagy and apoptosis. Thus, the impact of NSP1 on creating an intracellular environment favorable to virus replication may extend well beyond the IFN signaling pathway.

Source: Microbial Cell

DOI: 10.15698/mic2017.11.600

Authors: Kaitlin A. Davis, John T. Patton

Institutions: Johns Hopkins University, Indiana University Bloomington, Indiana University

Language: English

Topic: interferon and immune responses

Subfield: Immunology

Field: Immunology and Microbiology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: gold

Estimated APC paid: $1,283