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The interplay between NOD2 and TLR2 following recognition of components of the bacterial cell wall peptidoglycan is well-established, however their role in redirecting metabolic pathways in myeloid cells to degrade pathogens and mount antigen presentation remains unclear. We show NOD2 and TLR2 mediate phosphorylation of the deubiquitinase ataxin-3 via RIPK2 and TBK1. In myeloid cells ataxin-3 associates with the mitochondrial cristae protein MIC60, and is required for oxidative phosphorylation. Depletion of ataxin-3 leads to impaired induction of mitochondrial reactive oxygen species (mROS) and defective bacterial killing. A mass spectrometry analysis of NOD2/TLR2 triggered ataxin-3 deubiquitination targets revealed immunometabolic regulators, including HIF-1α and LAMTOR1 that may contribute to these effects. Thus, we define how ataxin-3 plays an essential role in NOD2 and TLR2 sensing and effector functions in myeloid cells.

Original publication

DOI

10.3389/fimmu.2019.01495

Type

Journal article

Journal

Front Immunol

Publication Date

2019

Volume

10

Keywords

Nod2, TLR2, ataxin 3, innate immnuity, metabolism, Ataxin-3, Cell Respiration, HEK293 Cells, Humans, Immunity, Innate, Mitochondria, Myeloid Cells, Nod2 Signaling Adaptor Protein, Phosphorylation, Protein-Serine-Threonine Kinases, Reactive Oxygen Species, Receptor-Interacting Protein Serine-Threonine Kinase 2, Signal Transduction, THP-1 Cells, Toll-Like Receptor 2