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BAP1 ubiquitinates Histone_H2A. 7 / 7
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"Genomic analyses together with robust statistics have revealed that the restoration of BAP1 facilitates the formation of the polycomb repressive deubiquitinase (PR-DUB) complex and inhibits ubiquitinated histone 2A (H2Aub) occupancy on the SLC7A11 promoter."
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"BRCA1-associated protein 1 (BAP1) [18], the crucial constituent of the deubiquitinase complex, attenuated the initiation and extension of SLC7A11 transcription by deubiquitinating histone 2A, while the steady-state levels and half-life of SLC7A11 were improved by combination with the ovarian tumor family member deubiquitinase (OTUB1) [19]."
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"Several studies have revealed that BAP1 can inhibit ubiquitinated histone 2A (H2Aub) occupancy on the SLC7A11 promoter (Zhang et al., 2018)."
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"The mechanism may be that BAP1 suppresses SLC7A11 transcription by reducing histone 2A ubiquitination (H2Aub) on the SLC7A11 gene."
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"Moreover, the tumor suppressor gene, BRCA1-associated protein 1 (BAP1), was found to reduce SLC7A11 expression by decreasing histone 2A ubiquitination occupancy on its promoter in human cancer, which consequently resulted in increased ferroptosis (Zhang et al., 2018)."
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"The tumour suppressor BRCA1-associated protein 1 (BAP1) is a nuclear deubiquitinating enzyme and can reduce histone 2A ubiquitination (H2Aub) on chromatin."
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"BAP1 mediated deubiquitination of histone 2A ubiquitination (H2Aub), while monoubiquitination of histone H2B on lysine 120 (H2Bub1) induced the expression of SLC7A11 during ferroptosis and consequentl[MISSING/INVALID CREDENTIALS: limited to 200 char for Elsevier]"
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