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• W2094920145 abstract "The TRIpartite Motif (TRIM) family of RING-domain-containing proteins participate in a variety of cellular functions. The β-transducin repeat-containing protein (β-TrCP), a component of the Skp-Cullin-F-box-containing (SCF) E3 ubiquitin ligase complex, recognizes the NF-κB inhibitor IκBα and precursor p100 for proteasomal degradation and processing, respectively. β-TrCP thus plays a critical role in both canonical and non-canonical NF-κB activation. Here we report that TRIM9 is a negative regulator of NF-κB activation. Interaction between the phosphorylated degron motif of TRIM9 and the WD40 repeat region of β-TrCP prevented β-TrCP from binding its substrates, stabilizing IκBα and p100 and thereby blocking NF-κB activation. Consequently, expression or depletion of the TRIM9 gene significantly affected NF-κB-induced inflammatory cytokine production. This study not only elucidates a mechanism for TRIM9-mediated regulation of the β-TrCP SCF complex activity but also identifies TRIM9 as a brain-specific negative regulator of the NF-κB pro-inflammatory signalling pathway." @default.
• W2094920145 created "2016-06-24" @default.
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• W2094920145 date "2014-09-05" @default.
• W2094920145 modified "2023-10-18" @default.
• W2094920145 title "Negative regulation of NF-κB activity by brain-specific TRIpartite Motif protein 9" @default.
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• W2094920145 doi "https://doi.org/10.1038/ncomms5820" @default.
• W2094920145 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4157316" @default.
• W2094920145 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25190485" @default.
• W2094920145 hasPublicationYear "2014" @default.
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