IndraLab

"Importantly, the tumor suppressor p14ARF compromises the Hdm2-YY1 interaction, which is important for YY1 regulation of p53."

"We identify direct physical interactions of YY1 with Hdm2 and p53 and show that the basis for YY1-regulating p53 ubiquitination is its ability to facilitate Hdm2-p53 interaction."

"Interestingly, Yy1 can form transcription factor complex with both p53 and Mdm2 (), suggesting that Yy1 indirectly regulates p53-dependent cell cycle regulation leading to eventual sequestration of p5[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

"YY1 directly interacts with both p53 and Mdm2, a ubiquitin E3 ligase, and enhances Mdm2-mediated p53 ubiquitination and degradation. xref , xref YY1 depletion leads to either apoptosis or cell cycle arrest, depending on the cell types. xref , xref , xref Importantly, this regulation is independent of the transcriptional activity of YY1 because a YY1 mutant deficient in DNA binding retains the ability to stimulate p53 ubiquitination, and purified YY1 protein can promote p53 ubiquitination in vitro . xref A previous study indicated that YY1 promotes the expression of cytochrome c oxidase subunit 7C, regulating mitochondrial respiration. xref Recently, Yu et al xref demonstrated that this activation is mediated by the YY1-recruited deubiquitination enzyme BAP1 to the cytochrome c oxidase subunit 7C promoter."

"201–295, mainly 226–295, xref ), and because YY1 and Hdm2 interact with p53 through different regions (a."

"YY1 forms a ternary complex with Mdm2 and p53 to promote Mdm2-mediated p53 ubiquitination and degradation. xref In addition, YY1 interacts with many other proteins directly regulating tumorigenesis."

"YY1 directly binds to both Hdm2 and p53 and enhances p53 ubiquitination and degradation, thus YY1 is a negative regulator of p53 ( xref )."