IndraLab

Statements

SUV39H1 binds USP7 and MDM2. 7 / 7
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reach
"Whether this protection occurs on p53 target promoters alone and/or elsewhere within the cell as well as the physiological significance of these interactions in a p53 null context remain to be elucida[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
26971997
sparser
"USP7 forms a trimeric protein complex with SUV39H1 and MDM2."
26971997
sparser
"Collectively, these results indicate that shared physical interactions of USP7 and SUV39H1 with MDM2 are required either for USP7 to deubiquitinate SUV39H1 or for MDM2 to ubiquitinate SUV39H1, both re[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
26971997
reach
"Our present findings as well as data available from previous reports indicate that ' basal ' levels of mostly transcriptionally inactive p53 enable the recruitment of the USP7, MDM2, and SUV39H1 complex to p53 REs via p53-MDM2 interaction, placing the H3K9me3 repressive mark and maintaining low basal transcription activity of p53 target genes (XREF_FIG)."
26971997
reach
"Our present studies demonstrate that USP7, SUV39H1 and MDM2 exist in a trimeric complex and that the USP7, MDM2, and SUV39H1 complex keeps MDM2 inactive under basal conditions."
26971997
sparser
"Collectively, these results indicate that shared physical interactions of USP7 and SUV39H1 with MDM2 are required for either for USP7 to deubiquitinate SUV39H1 or for MDM2 to ubiquitinate SUV39H1; both resulting in enhanced SUV39H1 stability."
26971997
sparser
"Mechanistically, USP7 forms a trimeric complex with MDM2 and SUV39H1, independent of DNA, and modulates MDM2-dependent SUV39H1 ubiquitination."
26971997