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Status |
Public on Jul 29, 2011 |
Title |
The tumor antigen PRAME is a substrate recognition subunit of a Cul2-based ubiquitin ligase and is associated with active NFY promoters |
Organism |
Homo sapiens |
Experiment type |
Genome binding/occupancy profiling by high throughput sequencing Expression profiling by high throughput sequencing
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Summary |
The human tumor antigen PRAME (Preferentially expressed antigen of melanoma) is frequently overexpressed in tumors. High PRAME levels correlate with poor clinical outcome of several cancers, but the mechanisms by which PRAME could be involved in tumorigenesis remain largely elusive. We applied protein-complex purification strategies and identified PRAME as a substrate recognition subunit of a Cullin2-based E3 ubiquitin ligase. Genome-wide chromatin immunoprecipitation experiments revealed that PRAME is specifically enriched at NF-Y promoters that are transcriptionally active, suggesting a role in gene activation. Our results are consistent with the involvement of the PRAME ubiquitin ligase complex in NF-Y-mediated transcriptional regulation.
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Overall design |
ChIP-seq binding profiles of PRAME (ChIP-seq using the preimmune serum was used as negative control), NFYA, and NFYB, and expression analysis by RNA-seq in K562 human leukemia cell line
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Contributor(s) |
Costessi A, Stunnenberg HG |
Citation(s) |
21822215 |
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Submission date |
Jan 04, 2011 |
Last update date |
May 15, 2019 |
Contact name |
H.G. Stunnenberg |
E-mail(s) |
[email protected]
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Phone |
+31-24-3610520
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Organization name |
Radboud University
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Department |
Department of Molecular Biology (274)
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Street address |
Geert Grooteplein 28
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City |
Nijmegen |
ZIP/Postal code |
6525 GA |
Country |
USA |
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Platforms (1) |
GPL9115 |
Illumina Genome Analyzer II (Homo sapiens) |
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Samples (5)
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Relations |
BioProject |
PRJNA136821 |
SRA |
SRP005174 |