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Cross-talk between SUMOylation and ISGylation in response to interferon.

Abstract：

:Interferon (IFN) plays a central role in regulating host immune response to viral pathogens through the induction of IFN-Stimulated Genes (ISGs). IFN also enhances cellular SUMOylation and ISGylation, though the functional interplay between these modifications remains unclear. Here, we used a system-level approach to profile global changes in protein abundance in SUMO3-expressing cells stimulated by IFNα. These analyses revealed the stabilization of several ISG factors including SAMHD1, MxB, GBP1, GBP5, Tetherin/BST2 and members of IFITM, IFIT and IFI families. This process was correlated with enhanced IFNα-induced anti-HIV-1 and HSV-1 activities. Also IFNα upregulated protein ISGylation through increased abundance of E2 conjugating enzyme UBE2L6, and E3 ISG15 ligases TRIM25 and HERC5. Remarkably, TRIM25 depletion blocked SUMO3-dependent protein stabilization in response to IFNα. Our data identify a new mechanism by which SUMO3 regulates ISG product stability and reinforces the relevance of the SUMO pathway in controlling both the expression and functions of the restriction factors and IFN antiviral response.

journal_name

Cytokine

journal_title

Cytokine

authors

El-Asmi F,McManus FP,Brantis-de-Carvalho CE,Valle-Casuso JC,Thibault P,Chelbi-Alix MK

doi

10.1016/j.cyto.2020.155025

subject

Has Abstract

pub_date

2020-05-01 00:00:00

pages

155025

eissn

1043-4666

issn

1096-0023

pii

S1043-4666(20)30041-7

journal_volume

129

pub_type

杂志文章

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