IndraLab

Statements

USP16 leads to the phosphorylation of NFKB1. 11 / 11
| 5 6
reach
"This observation raised a critical question regarding whether USP16 directly regulates IKKbeta activity or p105 phosphorylation."
| PMC
sparser
"USP16 specifically promotes p105 phosphorylation."
| PMC
reach
"USP16 specifically promotes p105 phosphorylation."
| PMC
reach
"In these reconstituted USP16 -/- fibroblasts, USP16 WT, but not USP16 CI, rescued the phosphorylation of p105 and the interaction between IKKbeta and p105 (XREF_FIG)."
| PMC
reach
"With IKKbeta K238R, USP16 silencing no longer impaired the phosphorylation of p105."
| PMC
sparser
"The deubiquitinating enzyme USP16 can promote the interaction between IKKβ and p105 and phosphorylate p105 by selectively removing K33-linked polyubiquitin chains from IKKβ, thereby activating the NF-κB signaling pathway and promoting intestinal inflammation [ xref ]."
39420190
sparser
"The deubiquitinating enzyme USP16 can promote the interaction between IKKβ and p105 and phosphorylate p105 by selectively removing K33-linked polyubiquitin chains from IKKβ, thereby activating the NF-κB signaling pathway and promoting intestinal inflammation [ xref ]."
39420190
sparser
"The deubiquitinating enzyme USP16 can promote the interaction between IKKβ and p105 and phosphorylate p105 by selectively removing K33-linked polyubiquitin chains from IKKβ, thereby activating the NF-κB signaling pathway and promoting intestinal inflammation [ xref ]."
39420190
reach
"Collectively, these data indicated that the USP16 mediated deubiquitination of IKKbeta may be specifically involved in the phosphorylation and processing of p105."
| PMC
sparser
"USP16 specifically promotes p105 phosphorylation."
| PMC
sparser
"USP16 specifically promotes p105 phosphorylation."
| PMC