IndraLab

Statements


USP7 deubiquitinates NFkappaB. 7 / 7
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"It has been reported that deubiquitination of NF-kappaB by USP7 is essential for TLR- and TNFR induced gene expression [XREF_BIBR], thus USP7 may has a positive feedback in regulating TNFR1 and also circ-DB formation."

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"These findings reveal a unique mechanism controlling NF-kappaB activity and demonstrate that the deubiquitination of NF-kappaB by USP7 is critical for target gene transcription."

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"NFkappaB can be directly deubiquitinated by HAUSP 87 or can be indirectly regulated by deubiquitination of its upstream factors, such as TRAF6, 24 NEMO (IKK-gamma) XREF_BIBR, XREF_BIBR (HSCARG interacts with NEMO to suppress its polyubiquitination by recruiting HAUSP 91), NIMA (Never In Mitosis Gene A)-related kinase 2 (Nek2), a centrosomal serine/threonine kinase (HAUSP stabilizes Nek2 leading to activation of NFkappaB pathway in multiple myeloma)."

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"USP7 deubiquitination of NF-kappaB leads to increased transcription."

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"Therefore, USP7 's deubiquitination of NF-kappaB enhances pro cytokine production when induced by the TLR signaling pathway."

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"This analysis reveals a significant and selective inhibition of NF-kB target gene expression following TLR4 activation and strongly supports the inhibition of USP7 deubiquitination of NF-kB as a potential therapeutic strategy."

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"Moreover, USP7 deubiquitination of NF-kappaB subunits leads to the increase of transcriptional activity, suggesting this may be the mechanism by which P22077 inhibits H 2 O 2 -induced USP7 mRNA expression."