IndraLab

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USP14 deubiquitinates NLRC5. 6 / 7
1 | 6

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"The ubiquitination of NLRC5 could be reversely regulated by USP14."

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"Mechanistically, USF1 functioned as a transcriptional activator of USP14 that caused de-ubiquitination of NLRC5, resulting in Smad2/3 pathway activation and EndMT induction in ox-LDL-exposed HUVECs."

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"In this study, we verified that USP14 enhanced NLRC5 protein level via de-ubiquitination of NLRC5."

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"Next, we determined whether USP14 inhibited NLRC5 ubiquitination through its DUB activity."

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"These results suggest that USP14 inhibits NLRC5 ubiquitination through its DUB activity."

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"In an effort to elucidate the mechanisms underlying this regulation, the Cui group showed that TLR4 stimulation activates the TRAF2/6 complex, which ubiquitinates NLRC5 on Lys1178 residue, presumably leading to its degradation and release of IKKalpha and IKKbeta to complex with IKKgamma [XREF_BIBR, XREF_BIBR] (XREF_FIG) This study also showed that the ubiquitin specific protease 14 (USP14) deubiquitinates NLRC5 to sustain the NLRC5 mediated inhibition of NF-kappaB activation."