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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
21-22
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pubmed:dateCreated |
2008-9-15
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pubmed:abstractText |
We have recently reported that poly-SUMO-2/3 conjugates are subject to a ubiquitin-dependent proteolytic control in human cells. Here we show that arsenic trioxide (ATO) increases SUMO-2/3 modification of promyelocytic leukemia (PML) leading to its subsequent ubiquitylation in vivo. The SUMO-binding ubiquitin ligase RNF4 mediates this modification and causes disruption of PML nuclear bodies upon treatment with ATO. Reconstitution of SUMO-dependent ubiquitylation of PML by RNF4 in vitro and in a yeast trans vivo system revealed a preference of RNF4 for chain forming SUMOs. Polysumoylation of PML in response to ATO thus leads to its recognition and ubiquitylation by RNF4.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antineoplastic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Arsenicals,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oxides,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/RNF4 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SUMO2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SUMO3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Small Ubiquitin-Related Modifier...,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins,
http://linkedlifedata.com/resource/pubmed/chemical/arsenic trioxide
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
22
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pubmed:volume |
582
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3174-8
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pubmed:meshHeading |
pubmed-meshheading:18708055-Antineoplastic Agents,
pubmed-meshheading:18708055-Arsenicals,
pubmed-meshheading:18708055-Cell Line, Tumor,
pubmed-meshheading:18708055-Down-Regulation,
pubmed-meshheading:18708055-Humans,
pubmed-meshheading:18708055-Leukemia, Promyelocytic, Acute,
pubmed-meshheading:18708055-Nuclear Proteins,
pubmed-meshheading:18708055-Oxides,
pubmed-meshheading:18708055-Proteasome Endopeptidase Complex,
pubmed-meshheading:18708055-Small Ubiquitin-Related Modifier Proteins,
pubmed-meshheading:18708055-Transcription Factors,
pubmed-meshheading:18708055-Ubiquitination,
pubmed-meshheading:18708055-Ubiquitins
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pubmed:year |
2008
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pubmed:articleTitle |
Arsenic trioxide stimulates SUMO-2/3 modification leading to RNF4-dependent proteolytic targeting of PML.
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pubmed:affiliation |
Center for Molecular Medicine Cologne (CMMC), Institute for Genetics, Zülpicher Strasse 47, 50674 Köln, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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