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• W2578139436 startingPage "307" @default.
• W2578139436 abstract "Ubiquitination is a versatile post-translational modification involved in nuclear factor-κB (NF-κB) activation of Toll-like receptor (TLR) signaling. Here, we demonstrated that Trim13, an E3 ubiquitin ligase, is up-regulated in macrophages upon stimulation with TLR2 ligand. Knockdown of Trim13 attenuated TLR2-mediated production of cytokines/chemokines and formation of foam cells as well as activation of NF-κB. Trim13 interacts with tumor necrosis factor receptor-associated factor 6 (TRAF6) and potentiates NF-κB activity via ubiquitination of TRAF6. Overexpression of inactive mutant (C10/13A) or really interesting new gene (RING) deletion mutant of Trim13 did not potentiate ubiquitination of TRAF6 or activation of NF-κB. These results suggest that the effects of Trim13 are dependent on its E3 ligase activity. Trim13 used K29-linked polyubiquitin chains for TRAF6 ubiquitination to promote NF-κB activity and thus potentiated activation of TLR2-mediated immune responses. Our data identify Trim13 as a positive regulator of NF-κB activation and suggest that K29-linked polyubiquitination is a specific ubiquitin-linked pattern involved in the control of TLR2 signaling." @default.
• W2578139436 created "2017-01-26" @default.
• W2578139436 creator A5033136222 @default.
• W2578139436 creator A5063462351 @default.
• W2578139436 date "2017-01-13" @default.
• W2578139436 modified "2023-10-07" @default.
• W2578139436 title "Trim13 Potentiates Toll-Like Receptor 2–Mediated Nuclear Factor <i>κ</i>B Activation via K29-Linked Polyubiquitination of Tumor Necrosis Factor Receptor-Associated Factor 6" @default.
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• W2578139436 doi "https://doi.org/10.1124/mol.116.106716" @default.
• W2578139436 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28087809" @default.
• W2578139436 hasPublicationYear "2017" @default.
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