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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
21
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pubmed:dateCreated |
2006-5-18
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pubmed:abstractText |
The promyelocytic leukemia gene was first identified through its fusion to the gene encoding the retinoic acid receptor alpha (RARalpha) in acute promyelocytic leukemia (APL) patients. The promyelocytic leukemia gene product (PML) becomes conjugated in vivo to the small ubiquitin-like protein SUMO-1, altering its behavior and capacity to recruit other proteins to PML nuclear bodies (PML-NBs). In the NB4 cell line, which was derived from an APL patient and expresses PML:RARalpha, we observed a retinoic acid-dependent change in the modification of specific proteins by SUMO-1. To dissect the interaction of PML with the SUMO-1 modification pathway, we used the budding yeast Saccharomyces cerevisiae as a model system through expression of PML and human SUMO-1 (hSUMO-1). We found that PML stimulated hSUMO-1 modification in yeast, in a manner that was dependent upon PML's RING-finger domain. PML:RARalpha also stimulated hSUMO-1 conjugation in yeast. Interestingly, however, PML and PML:RARalpha differentially complemented yeast Smt3p conjugation pathway mutants. These findings point toward a potential function of PML and PML:RARalpha as SUMO E3 enzymes or E3 regulators, and suggest that fusion of RARalpha to PML may affect this activity.
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pubmed:grant |
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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/CDC11 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Multiprotein Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nocodazole,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oncogene Proteins, Fusion,
http://linkedlifedata.com/resource/pubmed/chemical/PML protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SMT3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SUMO-1 Protein,
http://linkedlifedata.com/resource/pubmed/chemical/SUMO1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Siz1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Siz2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Small Ubiquitin-Related Modifier...,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tretinoin,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/promyelocytic leukemia-retinoic...
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0950-9232
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2999-3005
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pubmed:dateRevised |
2009-7-23
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pubmed:meshHeading |
pubmed-meshheading:16501610-Amino Acid Substitution,
pubmed-meshheading:16501610-Cell Cycle Proteins,
pubmed-meshheading:16501610-Cell Line, Tumor,
pubmed-meshheading:16501610-Cytoskeletal Proteins,
pubmed-meshheading:16501610-Genetic Complementation Test,
pubmed-meshheading:16501610-Humans,
pubmed-meshheading:16501610-Leukemia, Promyelocytic, Acute,
pubmed-meshheading:16501610-Multiprotein Complexes,
pubmed-meshheading:16501610-Mutagenesis, Site-Directed,
pubmed-meshheading:16501610-Neoplasm Proteins,
pubmed-meshheading:16501610-Nocodazole,
pubmed-meshheading:16501610-Nuclear Proteins,
pubmed-meshheading:16501610-Oncogene Proteins, Fusion,
pubmed-meshheading:16501610-Protein Structure, Tertiary,
pubmed-meshheading:16501610-Recombinant Fusion Proteins,
pubmed-meshheading:16501610-Repressor Proteins,
pubmed-meshheading:16501610-SUMO-1 Protein,
pubmed-meshheading:16501610-Saccharomyces cerevisiae,
pubmed-meshheading:16501610-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:16501610-Small Ubiquitin-Related Modifier Proteins,
pubmed-meshheading:16501610-Species Specificity,
pubmed-meshheading:16501610-Transcription Factors,
pubmed-meshheading:16501610-Transfection,
pubmed-meshheading:16501610-Tretinoin,
pubmed-meshheading:16501610-Tumor Suppressor Proteins,
pubmed-meshheading:16501610-Ubiquitin-Protein Ligases
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pubmed:year |
2006
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pubmed:articleTitle |
The promyelocytic leukemia protein stimulates SUMO conjugation in yeast.
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pubmed:affiliation |
Section on Cell Cycle Regulation, Laboratory of Gene Regulation and Development, NICHD/NIH, Bethesda, MD 20892, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, N.I.H., Intramural
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