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Journal articles

Interferon controls SUMO availability via the Lin28 and let-7 axis to impede virus replication

Abstract : Small ubiquitin-related modifier (SUMO) protein conjugation onto target proteins regulates multiple cellular functions, including defence against pathogens, stemness and senescence. SUMO1 peptides are limiting in quantity and are thus mainly conjugated to high-affinity targets. Conjugation of SUMO2/3 paralogues is primarily stress inducible and may initiate target degradation. Here we demonstrate that the expression of SUMO1/2/3 is dramatically enhanced by interferons through an miRNA-based mechanism involving the Lin28/let-7 axis, a master regulator of stemness. Normal haematopoietic progenitors indeed display much higher SUMO contents than their differentiated progeny. Critically, SUMOs contribute to the antiviral effects of interferons against HSV1 or HIV. Promyelocytic leukemia (PML) nuclear bodies are interferon-induced domains, which facilitate sumoylation of a subset of targets. Our findings thus identify an integrated interferon-responsive PML/SUMO pathway that impedes viral replication by enhancing SUMO conjugation and possibly also modifying the repertoire of targets. Interferon-enhanced post-translational modifications may be essential for senescence or stem cell self-renewal, and initiate SUMO-dependent proteolysis.
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Contributor : Valérie Lallemand-Breitenbach Connect in order to contact the contributor
Submitted on : Wednesday, January 15, 2020 - 12:00:54 PM
Last modification on : Friday, April 29, 2022 - 11:10:08 AM

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Umut Sahin, Omar Ferhi, Xavier Carnec, Alessia Zamborlini, Laurent Peres, et al.. Interferon controls SUMO availability via the Lin28 and let-7 axis to impede virus replication. Nature Communications, Nature Publishing Group, 2014, 5, pp.4187. ⟨10.1038/ncomms5187⟩. ⟨inserm-02440658⟩



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