IndraLab

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JOSD2 is ubiquitinated. 4 / 4
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"Concurrently, mutant KRAS suppresses E3 ubiquitin ligase-mediated ubiquitination and degradation of JOSD2 via a positive feedback loop, thereby driving malignant proliferation in CRC. xref Moreover, Cui et al. reported that in patients with very early-onset inflammatory bowel disease (VEO-IBD) harboring the novel NLRP3 R779C mutation, the NLRP3-R779C variant exhibited reduced ubiquitination levels compared to wild-type NLRP3 (NLRP3-WT) due to deubiquitination by BRCC3 and JOSD2 in macrophages. xref This enhances inflammasome activity, exacerbating pro-inflammatory cytokine release and pyroptosis."
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"Considering that E3 ligases are key proteins regulating the ubiquitination levels of substrates, we guessed whether KRAS mutants regulate JOSD2 ubiquitination through their E3 ligases."
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"Reciprocally, the stabilized KRAS mutants inhibit the ubiquitination of JOSD2 by suppressing its bona fide E3 ubiquitin ligase CHIP, thus forming a JOSD2/KRAS positive feedback circuit that robustly accelerates proliferation in KRAS-mutant CRC cells."
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"Moreover, EGF stimulation induced KRAS activation also posed a similar effect (Supplementary Fig.  xref ), demonstrating the regulation of KRAS on JOSD2 ubiquitination depending on KRAS activity."
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