The tumour antigen PRAME is a subunit of a Cul2 ubiquitin ligase and associates with active NFY promoters

Adalberto Costessi, Nawel Mahrour, Esther Tijchon, Rieka Stunnenberg, Marieke A. Stoel, Pascal W. Jansen, Dotan Sela, Skylar Martin-Brown, Michael P. Washburn, Laurence Florens, Joan W. Conaway, Ronald C. Conaway, Hendrik G. Stunnenberg

Research output: Contribution to journalArticlepeer-review

43 Scopus citations

Abstract

The human tumour antigen PRAME (preferentially expressed antigen of melanoma) is frequently overexpressed in tumours. High PRAME levels correlate with poor clinical outcome of several cancers, but the mechanisms by which PRAME could be involved in tumourigenesis remain largely elusive. We applied protein-complex purification strategies and identified PRAME as a substrate recognition subunit of a Cullin2-based E3 ubiquitin ligase. PRAME can be recruited to DNA in vitro, and genome-wide chromatin immunoprecipitation experiments revealed that PRAME is specifically enriched at transcriptionally active promoters that are also bound by NFY and at enhancers. Our results are consistent with a role for the PRAME ubiquitin ligase complex in NFY-mediated transcriptional regulation.

Original languageEnglish (US)
Pages (from-to)3786-3798
Number of pages13
JournalEMBO Journal
Volume30
Issue number18
DOIs
StatePublished - Sep 2011
Externally publishedYes

Keywords

  • Cullin2
  • NFY
  • PRAME
  • transcription
  • ubiquitination

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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