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Interferon, restriction factors and SUMO pathways.

Authors
  • El-Asmi, Faten1
  • McManus, Francis P2
  • Thibault, Pierre3
  • Chelbi-Alix, Mounira K4
  • 1 INSERM UMR-S 1124, Université Paris Descartes, 45 rue des Saints Pères, 75006, Paris, France. , (France)
  • 2 Institute for Research in Immunology and Cancer, Quebec, Canada. , (Canada)
  • 3 Institute for Research in Immunology and Cancer, Quebec, Canada; University of Montreal, Department of Chemistry, Quebec, Canada. , (Canada)
  • 4 INSERM UMR-S 1124, Université Paris Descartes, 45 rue des Saints Pères, 75006, Paris, France. Electronic address: mounira.chelb[email protected] , (France)
Type
Published Article
Journal
Cytokine & growth factor reviews
Publication Date
Oct 01, 2020
Volume
55
Pages
37–47
Identifiers
DOI: 10.1016/j.cytogfr.2020.03.001
PMID: 32591223
Source
Medline
Keywords
Language
English
License
Unknown

Abstract

SUMOylation is a reversible post-translational modification that regulates several cellular processes including protein stability, subcellular localization, protein-protein interactions and plays a key role in the interferon (IFN) pathway and antiviral defense. In human, three ubiquitously expressed SUMO paralogs (SUMO1, 2 and 3) have been described for their implication in both intrinsic and innate immunity. Differential effects between SUMO paralogs are emerging such as their distinctive regulations of IFN synthesis, of IFN signaling and of the expression and function of IFN-stimulated gene (ISG) products. Several restriction factors are conjugated to SUMO and their modifications are further enhanced in response to IFN. Also, IFN itself was shown to increase global cellular SUMOylation and requires the presence of the E3 SUMO ligase PML that coordinates the assembly of PML nuclear bodies. This review focuses on differential effects of SUMO paralogs on IFN signaling and the stabilization/destabilization of ISG products, highlighting the crosstalk between SUMOylation and other post-translational modifications such as ubiquitination and ISGylation. Copyright © 2020 The Authors. Published by Elsevier Ltd.. All rights reserved.

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