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USP22 deubiquitinates Histone_H2B. 16 / 16
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"As we discussed previously, USP22 is a component of a transcriptional activator complex SAGA and can deubiquitinate histones H2A and H2B, as well as several other substrates (Zhang et al., 2008a, b)."

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"USP22 is a component of the SAGA transcriptional coactivator complex and can deubiquitinate H2A and H2B [XREF_BIBR - XREF_BIBR]."

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"USP22 deubiquitylates both, H2A and H2B."

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"Remarkably, USP22, the human ortholog of Ubp8, forms a similar SAGA DUB module and deubiquitinates both H2A and H2B."

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"However, de-ubiquitylation of H2B by Usp22, the human homolog of yeast Ubp8, inhibits heterochromatic silencing and promotes gene activation [XREF_BIBR, XREF_BIBR]."

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"USP22 was initially reported to promote deubiquitylation of histones H2A and H2B, leading to transcription activation."

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"As a subunit of hSAGA, USP22 participates in the deubiquitination of histones H2A and H2B and the acetylation of histone H4 to regulate gene transcription and expression."

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"USP22 might de-ubiquitinate H2A and H2B, subunits of the human SAGA complex that are intimately linked to the transcriptional activation of the MYC gene and increased cell proliferation in HCC [XREF_BIBR]."

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"The requirement of ATXN7L3 for H2B deubiquitination by USP22, USP27x, and USP51 suggests that the ATXN7L3 zinc finger plays a role analogous to that of the Sgf11 zinc finger in docking human SAGA DUB [MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"USP22 may deubiquitinate H2A and H2B, subunits of the hSAGA complex that activate transcription factors and promote carcinogenesis [XREF_BIBR]."

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"USP22 forms part of the SAGA complex and requires the participation of cofactors like ATXN7L3 and ENY2 to deubiquitinate H2B, while USP27X functions independently of SAGA but also needs ATXN7L3 and ENY2 to act on H2B [8]."

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"USP22 is able to deubiquitinate histone H2A and H2B in vitro and is required for androgen receptor transcription activation."

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"The requirement of ATXN7L3 for H2B deubiquitination by USP22, USP27x, and USP51 suggests that all three use the ATXN7L3 zinc finger to dock the H2A and H2B acidic patch in a manner similar to that shown in the structure of the yeast DUB module bound to ubiquitinated nucleosomes."

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"Our observations regarding differentiation could not be correlated to H2B and H2Bub1 levels suggesting that H2B is only partially deubiquitinated by Usp22."

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"In yeast, the USP22 ortholog deubiquitylates H2B, resulting in Pol II Ser2 phosphorylation and subsequent transcriptional elongation."

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"In addition, reduced expression of USP22 is associated with chromosomal instability (CIN), since efficient chromosome compaction during mitosis requires USP22 deubiquitination of H2B in metaphase (Jeusset et al., 2021)."