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• W3203312792 endingPage "e202101137" @default.
• W3203312792 startingPage "e202101137" @default.
• W3203312792 abstract "Ubiquitination and phosphorylation are reversible posttranslational protein modifications regulating physiological and pathological processes. MAPK phosphatase (MKP)-1 regulates innate and adaptive immunity. The multifaceted roles of MKP-1 were attributed to dephosphorylation of p38 and JNK MAPKs. We show that the lack of MKP-1 modulates the landscape of ubiquitin ligases and deubiquitinase enzymes (DUBs). MKP-1-/- showed an aberrant regulation of several DUBs and increased expression of proteins and genes involved in IL-1/TLR signaling upstream of MAPK, including IL-1R1, IRAK1, TRAF6, phosphorylated TAK1, and an increased K63 polyubiquitination on TRAF6. Increased K63 polyubiquitination on TRAF6 was associated with an enhanced phosphorylated form of A20. Among abundant DUBs, ubiquitin-specific protease-13 (USP13), which cleaves polyubiquitin-chains on client proteins, was substantially enhanced in murine MKP-1-deficient BMDMs. An inhibitor of USP13 decreased the K63 polyubiquitination on TRAF6, TAK1 phosphorylation, IL-1β, and TNF-α induction in response to LPS in BMDMs. Our data show for the first time that MKP-1 modulates the ligase activity of TRAF6 through modulation of specific DUBs." @default.
• W3203312792 created "2021-10-11" @default.
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• W3203312792 date "2021-09-27" @default.
• W3203312792 modified "2023-10-11" @default.
• W3203312792 title "MKP-1 modulates ubiquitination/phosphorylation of TLR signaling" @default.
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• W3203312792 doi "https://doi.org/10.26508/lsa.202101137" @default.
• W3203312792 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8500224" @default.
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