IndraLab

Statements

USP22 binds ATXN7L3 and ENY2. 8 / 8
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"The SAGA DUB module is highly conserved both in subunit composition and structural organization ( xref ; xref ; xref ; xref ; xref ; xref ), The deubiquitinating enzyme USP22 (Ubp8 in yeast) closely associates with two adapter proteins, ATXN7L3 and ENY2 (Sgf11 and Sus1 in yeast, respectively) ( xref ; xref ; xref ), and a fourth protein, ATXN7 (Sgf73), anchors the DUB module to the larger SAGA complex."
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"It has been reported that USP22 interacts with ENY2 and ATXN7L3 and forms the transcriptional coactivator Spt-Ada-Gcn5-acetyltransferase (SAGA) complex to regulate global levels of H2B monoubiquitination, thereby promoting antibody class switch recombination by facilitating nonhomologous end joining ( xref ; xref ; xref )."
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"Similarly, USP22, the human homolog of Ubp8, is bound to the STAGA complex through interactions with ATXN7L3 and ENY2, which are homologs of Sgf11 and Sus1, respectively ( xref )."
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"Further, Pfam analysis of protein domain structures ( xref ) confirmed that in addition to the catalytic UCH domain, both USP27X and USP51 have an N-terminal Znf-UBP domain highly similar to that found in USP22, which is critical for USP22 interaction with ATXN7L3 and ENY2 and deubiquitination activity ( xref and xref ) ( xref )."
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"We show that the ubiquitin protease USP22 forms a subcomplex with ATXN7L3 (ySgf11 homolog) and ENY2 (ySus1 homolog)."
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"These results together suggest that ATXN7L3, USP22, and ENY2 form a stable subcomplex and that USP22 and ENY2 are recruited into TFTC/STAGA by ATXN7L3 ( Figure 2 D)."
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"Cotransfection and coimmunoprecipitation experiments revealed that the ATXN7L3 ZnF-Sgf11 domain alone is able to interact with both ENY2 and USP22 as efficiently as the full-length ATXN7L3 (see Figur[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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"Previous study has shown that USP22 interacts with ENY2 and ATXN7L3 and forms the transcriptional coactivator SAGA complex to regulate global levels of H2B monoubiquitination ( xref )."
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