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BAP1 is phosphorylated at serine 592 in S-phase following DNA damage.

ABSTRACT: The human BAP1 deubiquitinating enzyme is a chromatin-bound transcriptional regulator and tumor suppressor. BAP1 functions in suppressing cell proliferation, yet its role in the DNA damage response pathway is less understood. In this study we characterized DNA damage-induced phosphorylation of BAP1 at serine 592 (pS592) and the cellular outcomes of this modification. In contrast to the majority of BAP1, pS592-BAP1 is predominantly dissociated from chromatin. Our findings support a model whereby stress induced phosphorylation functions to displace BAP1 from specific promoters. We hypothesize that this regulates the transcription of a subset of genes involved in the response to DNA damage.

SUBMITTER: Eletr ZM

PROVIDER: S-EPMC3923164 | biostudies-literature | 2013 Dec

REPOSITORIES: biostudies-literature

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BAP1 is phosphorylated at serine 592 in S-phase following DNA damage.

Eletr Ziad M ZM Yin Luming L Wilkinson Keith D KD

FEBS letters 20131105 24

The human BAP1 deubiquitinating enzyme is a chromatin-bound transcriptional regulator and tumor suppressor. BAP1 functions in suppressing cell proliferation, yet its role in the DNA damage response pathway is less understood. In this study we characterized DNA damage-induced phosphorylation of BAP1 at serine 592 (pS592) and the cellular outcomes of this modification. In contrast to the majority of BAP1, pS592-BAP1 is predominantly dissociated from chromatin. Our findings support a model whereby ...[more]

PMID: 24211834

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