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

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.

Pubmed ID: 21822215

Authors

  • Costessi A
  • Mahrour N
  • Tijchon E
  • Stunnenberg R
  • Stoel MA
  • Jansen PW
  • Sela D
  • Martin-Brown S
  • Washburn MP
  • Florens L
  • Conaway JW
  • Conaway RC
  • Stunnenberg HG

Journal

The EMBO journal

Publication Data

September 14, 2011

Associated Grants

  • Agency: NIGMS NIH HHS, Id: R01 GM041628
  • Agency: NIGMS NIH HHS, Id: R37 GM41628

Mesh Terms

  • Antigens, Neoplasm
  • CCAAT-Binding Factor
  • Chromatin Immunoprecipitation
  • Cullin Proteins
  • Humans
  • Promoter Regions, Genetic
  • Protein Binding
  • Protein Subunits
  • Ubiquitin-Protein Ligases