Although initially identified in the suppressor of cytokine signaling (SOCS) family of proteins, the C-terminal SOCS box has now been identified in more than 40 proteins in nine different families. Growing evidence suggests that the SOCS box, similar to the F-box, acts as a bridge between specific substrate-binding domains and the more generic proteins that comprise a large family of E3 ubiquitin protein ligases. In this way, SOCS proteins regulate protein turnover by targeting proteins for polyubiquitination and, therefore, for proteasome-mediated degradation.
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Cullin-5 (Cul5) coordinates assembly of cullin-RING-E3 ubiquitin (Ub) ligase (CRL) complexes that include Suppressor of Cytokine Signaling (SOCS)-box-containing proteins. The SOCS-box proteins function to recruit specific substrates to the complex for ubiquitination and degradation. In hematopoiesis, SOCS-box proteins are best known for regulating the actions of cytokines that utilize the JAK-STAT signaling pathway.
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Article Synopsis
- E3 ubiquitin ligases play a crucial role in regulating antiviral immune responses during viral infections, particularly in response to RNA viruses.
- The study found that ASB3, an E3 ligase, is upregulated when RNA viruses like influenza A virus are present, and its overexpression inhibits type I interferon responses.
- Animals without ASB3 showed lower susceptibility to viral infections, as ASB3 promotes the degradation of MAVS, which is essential for antiviral signaling, highlighting ASB3's role as a negative regulator of immune responses.
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