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000163763 041__ $$aEnglish
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000163763 1001_ $$aAalto, Anna$$b0
000163763 245__ $$aM1-linked ubiquitination facilitates NF-κB activation and survival during sterile inflammation.
000163763 260__ $$aOxford [u.a.]$$bWiley-Blackwell$$c2022
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000163763 520__ $$aMethionine 1 (M1)-linked ubiquitination plays a key role in the regulation of inflammatory nuclear factor-κB (NF-κB) signalling and is important for clearance of pathogen infection in Drosophila melanogaster. M1-linked ubiquitin (M1-Ub) chains are assembled by the linear ubiquitin E3 ligase (LUBEL) in flies. Here, we have studied the role of LUBEL in sterile inflammation induced by different types of cellular stresses. We have found that the LUBEL catalyses formation of M1-Ub chains in response to hypoxic, oxidative and mechanical stress conditions. LUBEL is shown to be important for flies to survive low oxygen conditions and paraquat-induced oxidative stress. This protective action seems to be driven by stress-induced activation of the NF-κB transcription factor Relish via the immune deficiency (Imd) pathway. In addition to LUBEL, the intracellular mediators of Relish activation, including the transforming growth factor activating kinase 1 (Tak1), Drosophila inhibitor of apoptosis (IAP) Diap2, the IκB kinase γ (IKKγ) Kenny and the initiator caspase Death-related ced-3/Nedd2-like protein (Dredd), but not the membrane receptor peptidoglycan recognition protein (PGRP)-LC, are shown to be required for sterile inflammatory response and survival. Finally, we showed that the stress-induced upregulation of M1-Ub chains in response to hypoxia, oxidative and mechanical stress is also induced in mammalian cells and protects from stress-induced cell death. Taken together, our results suggest that M1-Ub chains are important for NF-κB signalling in inflammation induced by stress conditions often observed in chronic inflammatory diseases and cancer.
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000163763 650_7 $$2Other$$aNF-κB
000163763 650_7 $$2Other$$acell stress
000163763 650_7 $$2Other$$ahypoxia
000163763 650_7 $$2Other$$alinear ubiquitin chain
000163763 650_7 $$2Other$$asterile inflammation
000163763 650_2 $$2MeSH$$aAnimals
000163763 650_2 $$2MeSH$$aDrosophila: metabolism
000163763 650_2 $$2MeSH$$aDrosophila Proteins: genetics
000163763 650_2 $$2MeSH$$aDrosophila Proteins: metabolism
000163763 650_2 $$2MeSH$$aDrosophila melanogaster: metabolism
000163763 650_2 $$2MeSH$$aInflammation: genetics
000163763 650_2 $$2MeSH$$aMAP Kinase Kinase Kinases: metabolism
000163763 650_2 $$2MeSH$$aMammals: metabolism
000163763 650_2 $$2MeSH$$aMethionine: metabolism
000163763 650_2 $$2MeSH$$aNF-kappa B: genetics
000163763 650_2 $$2MeSH$$aNF-kappa B: metabolism
000163763 650_2 $$2MeSH$$aUbiquitin: metabolism
000163763 650_2 $$2MeSH$$aUbiquitination
000163763 7001_ $$aMartínez-Chacón, Gabriela$$b1
000163763 7001_ $$aKietz, Christa$$b2
000163763 7001_ $$aTsyganova, Nadezhda$$b3
000163763 7001_ $$aKreutzer, Joose$$b4
000163763 7001_ $$aKallio, Pasi$$b5
000163763 7001_ $$0P:(DE-2719)2810307$$aBroemer, Meike$$b6$$udzne
000163763 7001_ $$00000-0002-3878-2293$$aMeinander, Annika$$b7
000163763 773__ $$0PERI:(DE-600)2172518-4$$a10.1111/febs.16425$$gp. febs.16425$$n17$$p5180-5197$$tThe FEBS journal$$v289$$x0014-2956$$y2022
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