IndraLab

Statements

OTULIN ubiquitinates STAT1. 3 / 3
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"When OTULIN was knocked down, IFN-I was no longer able to induce downregulation of STAT1 linear ubiquitination (Fig. 5f), suggesting that IFN-I-mediated removal of STAT1 linear ubiquitination is dependent on OTULIN.Given that IFN-I signaling utilized OTULIN to remove linear ubiquitination of STAT1, we speculated that overexpression of OTULIN could promote the binding of STAT1 to IFNAR2 in IFN-I signaling."
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"OTULIN knockout inhibited downregulation of STAT1 linear ubiquitination induced by IFN-I, which further inhibited the binding of STAT1 to IFNAR2 and subsequent STAT1 activation."
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"Mutation of Lys511 and Lys652 of STAT1 abolished OTULIN-mediated regulation of STAT1 linear ubiquitination (Fig. 5d), suggesting that OTULIN could be a deubiquitinase that removes STAT1 linear ubiquitination."
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