IndraLab

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STAMBP leads to the ubiquitination of NLRP3. 4 / 4
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reach
"In this study, we demonstrate STAMBP-mediated ubiquitination of NLRP3 to provide a non- degradative signal, and STAMBP knockout increased IL-1β secretion in undifferentiated THP-1 monocytes (Fig. 2)."
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ubibrowser
"These findings describe a unique mechanism of non-degradative ubiquitination of <span class="match term1">NLRP3</span> by <span class="match term0">STAMBP</span> to limit excessive inflammasome activation and to reduce injurious IL-1beta signaling."
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sparser
"These findings describe a unique mechanism of non-degradative ubiquitination of NLRP3 by STAMBP to limit excessive inflammasome activation and to reduce injurious IL-1β signaling."
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reach
"Collectively, these data support a functional relationship via physical association of NLRP3 with STAMBP, whereby STAMBP modulates NLRP3 polyubiquitination through its catalytic activity."
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