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- W4313354584 abstract "Abstract NOD2 is a cytosolic pattern-recognition receptor that senses muramyl dipeptide of peptidoglycan that constitutes the bacterial cell wall, and plays an important role in maintaining immunological homeostasis in the intestine. To date, multiple molecules have shown to be involved in regulating NOD2 signaling cascades. p62 (sequestosome-1; SQSTM1) is a multifaceted scaffolding protein involved in trafficking molecules to autophagy, and regulating signal cascades activated by Toll-like receptors, inflammasomes and several cytokine receptors. Here, we show that p62 positively regulates NOD2-induced NF-kB activation and subsequent production of cytokines (IL-1b and TNF-a). p62 associated with the nucleotide binding domain of NOD2 through a bi-directional interaction mediated by either TRAF6-binding or ubiquitin-associated domains. NOD2 formed a large complex with p62 in an electron-dense area of the cytoplasm, which increased its signaling cascade likely through preventing its degradation. This study for the first time demonstrates a novel role of p62 in enhancing NOD2 signaling effects." @default.
- W4313354584 created "2023-01-06" @default.
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- W4313354584 date "2013-05-01" @default.
- W4313354584 modified "2023-10-14" @default.
- W4313354584 title "p62/SQSTM1 enhances NOD2-mediated signaling and cytokine production through stabilizing NOD2 oligomers (P4189)" @default.
- W4313354584 doi "https://doi.org/10.4049/jimmunol.190.supp.112.28" @default.
- W4313354584 hasPublicationYear "2013" @default.
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