IndraLab

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USP22 deubiquitinates H2Bub1. 7 / 7
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"Interestingly, neither free recombinant USP22 nor Ubp8p can efficiently deubiquitylate H2Bub1 or H2Aub1 (in the case of USP22) in vitro , indicating that an interaction(s) between the ZnF-UBP and othe[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"In addition, USP22 can also enhance DNA damage repair by deubiquitinating histones H2A and H2Bub1."

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"Thus, ATXN7L3 is required for the full activity of the three related DUB modules to regulate global H2Bub1 levels, whereas USP22-containing DUB module is less involved in genome-wide deubiquitylation of H2Bub1."

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"Along these lines it is interesting to note that neither free USP22 nor a stable recombinant subcomplex, composed of TAF5L, ATXN7L3, ENY2, and USP22, can deubiquitinate H2Aub1 or H2Bub1 in vitro, sugg[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"Finally, USP22 and the 2A-DUB (KIAA1915), both target H2Aub1 (although USP22 can also deubiquitylate H2Bub1), and both were described as co-activators of androgen receptor (AR)-mediated transcription."

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"Unlike the ATXN7L3 DUB complex, a USP22, ATXN7L3B, and ENY2 complex can not deubiquitinate H2Bub1 efficiently in vitro Moreover, ATXN7L3B knockdown inhibits migration of breast cancer cells in vitro and limits expression of ER target genes."

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"USP22, USP27X, or USP51 require ATXN7L3 and ENY2 for their full activity and are unable to deubiquitinate H2Bub1 alone."