IndraLab

Statements


USP22 is acetylated. 7 / 7
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sparser
"These results suggest that USP22 acetylation, incorporation into SAGA, or its deubiquitinase activity is unlikely contribute to its role as a barrier to reprogramming."

sparser
"USP22 is acetylated [ xref ], and USP7 is phosphorylated [ xref ]."

sparser
"In an attempt to separate the HAT activity from the DUB interaction domain to assess the contribution of both acetylation and deubiquitylation of PCAF and USP22, we generated an enzymatically dead PCAF by installing two mutations in the core HAT domain (PCAF-YFAA [Y616A/F617A] mutant) (; xref )."

sparser
"Furthermore, our data suggest that ATAC and SAGA control of gene transcription may be more specific than control of promoter H3K9 acetylation, indicating that specificity of transcriptional regulation by either complex may rely on unique effects of their additional enzymatic activities, namely H2B deubiquitination by USP22 and H4 acetylation by KAT14. xref Accordingly, our inspection of USP22 requirements in erythropoiesis suggest that they align with the stage specificity of SAGA but may exceed the effects of loss of SUPT20H and more directly resemble postcommitment contributions of KAT2A . Future studies investigating single and combined requirements of ATAC and SAGA enzymatic subunits in locus and cellular regulation will enhance our understanding of the transcriptional control of cell state and fate decisions, including in leukemia and the normal blood system."

sparser
"Interestingly, SIRT1 was identified as a mediator of acetylation of USP22 and the SAGA coactivator complex (Armour et al ., xref )."

sparser
"Interestingly, SIRT1 was also identified as a mediator of acetylation of USP22 and the SAGA coactivator complex [ xref ]."

sparser
"SIRT1 is a mediator of acetylation of the USP22 and SAGA coactivator complex."