Identification and molecular characterization of BP75, a novel bromodomain-containing protein

Edwin Cuppen, Marco Van Ham, Barry Pepers, Bé Wieringa, Wiljan Hendriks*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

28 Citations (Scopus)

Abstract

We here describe the identification and characterization of a novel bromodomain-containing protein, the bromodomain protein of 75 kDa (BP75). Initially, we identified BP75 in a two-hybrid screening for proteins that interact with the first PDZ (acronym for post-synaptic density protein PSD-95, Drosophila discs large tumor suppressor DlgA and the tight junction protein ZO-1) domain in protein tyrosine phosphatase-BAS-like (PTP-BL). We found that BP75 is expressed ubiquitously and show that both BP75 and a PTP-BL deletion mutant consisting of the first PDZ domain are located mainly in the nucleus, although cytoplasmic localization is also evident. Full-length PTP-BL, on the contrary, is predominantly localized in the cytoplasm, although some basal nuclear staining is observed. The described molecular interaction may reflect a mechanism of coupling submembraneous signalling events and nuclear events. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)291-298
Number of pages8
JournalFEBS letters
Volume459
Issue number3
DOIs
Publication statusPublished - 15 Oct 1999

Keywords

  • Bromodomain
  • Protein tyrosine phosphatase
  • Protein-protein interaction
  • Signalling

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