HOIL-1-catalysed, ester-linked ubiquitylation restricts IL-18 signaling in cytotoxic T cells but promotes TLR signalling in macrophages.

Tytuł:: HOIL-1-catalysed, ester-linked ubiquitylation restricts IL-18 signaling in cytotoxic T cells but promotes TLR signalling in macrophages.
Autorzy:: Petrova T; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life sciences, University of Dundee, UK.
Zhang J; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life sciences, University of Dundee, UK.
Nanda SK; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life sciences, University of Dundee, UK.
Figueras-Vadillo C; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life sciences, University of Dundee, UK.
Cohen P; MRC Protein Phosphorylation and Ubiquitylation Unit, School of Life sciences, University of Dundee, UK.
Źródło:: The FEBS journal [FEBS J] 2021 Oct; Vol. 288 (20), pp. 5909-5924. Date of Electronic Publication: 2021 May 06.
Typ publikacji:: Journal Article; Research Support, Non-U.S. Gov't
Język:: English
Imprint Name(s):: Original Publication: Oxford, UK : Published by Blackwell Pub. on behalf of the Federation of European Biochemical Societies, c2005-
MeSH Terms:: Ubiquitination*
Esters/*chemistry
Interleukin-18/*metabolism
Macrophages/*immunology
T-Lymphocytes, Cytotoxic/*immunology
Toll-Like Receptors/*metabolism
Ubiquitin/*chemistry
Ubiquitin-Protein Ligases/*physiology
Animals ; Interleukin-1 Receptor-Associated Kinases/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Signal Transduction
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Grant Information:: MR/R021406/1 United Kingdom MRC_ Medical Research Council; 209380/Z/17/Z United Kingdom WT_ Wellcome Trust
Contributed Indexing:: Keywords: HOIL-1; T cell; macrophage; myddosome; ubiquitylation
Substance Nomenclature:: 0 (Esters)
0 (Interleukin-18)
0 (Toll-Like Receptors)
0 (Ubiquitin)
EC 2.3.2.27 (Rbck1 protein, mouse)
EC 2.3.2.27 (Ubiquitin-Protein Ligases)
EC 2.7.11.1 (Interleukin-1 Receptor-Associated Kinases)
Entry Date(s):: Date Created: 20210501 Date Completed: 20211112 Latest Revision: 20211116
Update Code:: 20240105
DOI:: 10.1111/febs.15896
PMID:: 33932090
: Czasopismo naukowe

Pełny tekst

The atypical E3 ligase HOIL-1 forms ester bonds between ubiquitin and serine/threonine residues in proteins, but the physiological roles of this unusual modification are unknown. We now report that IL-18 signalling leading to the production of interferon γ (IFNγ) and granulocyte-macrophage colony-stimulating factor (GM-CSF) is enhanced in cytotoxic T cells from knock-in mice expressing the E3 ligase-inactive HOIL-1[C458S] mutant, demonstrating that the formation of HOIL-1-catalysed ester-linked ubiquitin bonds restricts the activation of this pathway. We show that the interaction of IRAK2 with TRAF6 is required for IL-18-stimulated IFN-γ and GM-CSF production, and that the increased production of these cytokines in cytotoxic T cells from HOIL-1[C458S] mice correlates with an increase in both the number and size of the Lys63/Met1-linked hybrid ubiquitin chains attached to IRAK2 in these cells. In contrast, the secretion of IL-12 and IL-6 and the formation of il-12 and il-6 mRNA induced in bone marrow-derived macrophages (BMDMs) by prolonged stimulation with TLR-activating ligands that signal via myddosomes, which also requires the interaction of IRAK2 with TRAF6, were not increased but modestly reduced in HOIL-1[C458S] BMDM. The decreased production of these cytokines correlated with reduced ubiquitylation of IRAK2. Our results establish that changes in HOIL-1-catalysed ester-linked ubiquitylation can promote or reduce cytokine production depending on the ligand, receptor and immune cell and may be explained by differences in the ubiquitylation of IRAK2.
(© 2021 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)

Comment in: FEBS J. 2021 Oct;288(20):5903-5908. (PMID: 34322999)

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