IndraLab

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USP44 deubiquitinates Histone_H2B. 8 / 8
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"Our results indicate that both the deubiquitination of histone H2B by USP44 and deacetylation of histone H3 by HDAC3 contribute to N-CoR mediated transcriptional repression (XREF_FIG)."

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"29 , 30 Of note, USP44 deubiquitinates histone H2B both in vivo and in vitro, which contributes to N‐CoR (USP44 is a part of the N‐CoR complex)‐mediated repression of target genes."

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"However, whether USP44 directly deubiquitinates histone H2B or how its activity is targeted to chromatin is not known."

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"As part of N-CoR, USP44 deubiquitinates H2B both in vivo and in vitro, and it contributes to N-CoR-mediated repression of target genes, including a genome integrated luciferase reporter (Vaquero et al[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"

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"USP44 within N-CoR deubiquitinates H2B in vitro and in vivo, and ablation of USP44 impairs the repressive activity of the N and CoR complex."

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"However, whether USP44 directly deubiquitinates histone H2B or how its activity is targeted to chromatin are not known."

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"USP44 negatively regulates H2B ubiquitination during embryonic stem cell development [XREF_BIBR]."

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"Our results indicate that both the deubiquitination of histone H2B by USP44 and deacetylation of histone H3 by HDAC3 contribute to N-CoR-mediated transcriptional repression."