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BAP1 is phosphorylated at serine 592 in S‐phase following DNA damage
Author(s) -
Eletr Ziad M.,
Yin Luming,
Wilkinson Keith D.
Publication year - 2013
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2013.10.035
Subject(s) - deubiquitinating enzyme , dna damage , serine , chromatin , phosphorylation , bap1 , microbiology and biotechnology , promoter , dna , chemistry , transcriptional regulation , dna repair , regulator , transcription (linguistics) , transcription factor , ubiquitin , biology , gene , gene expression , biochemistry , linguistics , philosophy
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.