IndraLab

Statements

USP22 activates H2Bub1. 9 / 9
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"The deubiquitinating enzyme USP22 catalyzes H2Bub1 removal in interphase and may also be required for H2Bub1 removal in early mitosis to maintain chromosome stability."
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"Mechanistically, reduced USP22 expression was determined to increase local H2Bub1 abundance at the inflammation regulator SPARC locus resulting in an increase in expression [ 161 ]."
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"Interestingly however, this compensatory mechanism does not function in all cellular processes in which USP22 mediated H2Bub1 regulation is involved, including transcriptional activation and DNA damage repair [XREF_BIBR, XREF_BIBR, XREF_BIBR] (see Section 6 and Section 9)."
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"To test this possibility, we sought to determine whether reduced USP22 expression impairs H2Bub1 removal specifically within prophase chromosomes."
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"Recently, USP22 depletion was also determined to impair H2Bub1 removal from mitotic chromosomes, inducing mitotic chromatin compaction defects and segregation errors that promote CIN [ 151 ]."
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"Using complementary genetic and QuantIM approaches, we show that USP22 silencing impairs H2Bub1 removal from chromosomes during prophase and correlates with increases in multiple CIN phenotypes."
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"Importantly, USP22 depletion decreases H2Bub1 abundance throughout the FOXP3 locus which corresponds with FOXP3 repression [ 207 ]."
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"Consistent with that finding is another study that implicates the ubiquitin protease, USP22, which targets H2Bub1 for turnover in malignant colon carcinoma."
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"Mechanistically, USP22 depletion in human CRC cells induced a profound upregulation of secreted protein acidic and rich in cysteine (SPARC) by affecting H3K27ac and H2Bub1 occupancy on the SPARC gene."
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