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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
7
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pubmed:dateCreated |
2004-6-18
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pubmed:abstractText |
Promyelocytic leukemia nuclear bodies (PML-NBs) comprise multiple regulatory factors and play crucial roles in the maintenance of cellular integrity, while unregulated activation of PML-NBs induces death and premature senescence. Hence, the function of PML-NBs must be directed properly; however, the mechanism that regulates PML-NBs remains unclear. In this paper, we show that PML-NBs are disintegrated by an AT-rich interaction domain family protein E2FBP1/hDril1 through specific desumoylation of promyelocytic leukemia protein (PML) in vivo and in vitro. RNA interference-mediated downregulation of E2FBP1/hDril1 results in hyperplasis of PML-NBs and consequent commitment to PML-dependent premature senescence. Thus, the function of E2FBP1/hDril1 is required for maintenance of survival potential of the cells. Our data suggest a novel mechanism to govern cellular integrity through the modulation of nuclear depots.
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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/ARID3A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescein-5-isothiocyanate,
http://linkedlifedata.com/resource/pubmed/chemical/Fluorescent Dyes,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin Heavy Chains,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Small Interfering,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1350-9047
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
11
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
747-59
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:15017387-Blotting, Western,
pubmed-meshheading:15017387-Cell Division,
pubmed-meshheading:15017387-Cell Nucleus Structures,
pubmed-meshheading:15017387-DNA-Binding Proteins,
pubmed-meshheading:15017387-Down-Regulation,
pubmed-meshheading:15017387-Escherichia coli,
pubmed-meshheading:15017387-Fluorescein-5-isothiocyanate,
pubmed-meshheading:15017387-Fluorescent Antibody Technique, Indirect,
pubmed-meshheading:15017387-Fluorescent Dyes,
pubmed-meshheading:15017387-Humans,
pubmed-meshheading:15017387-Immunoglobulin Heavy Chains,
pubmed-meshheading:15017387-KB Cells,
pubmed-meshheading:15017387-Leukemia, Promyelocytic, Acute,
pubmed-meshheading:15017387-Microscopy, Fluorescence,
pubmed-meshheading:15017387-Nuclear Proteins,
pubmed-meshheading:15017387-Oncogenes,
pubmed-meshheading:15017387-Precipitin Tests,
pubmed-meshheading:15017387-RNA, Small Interfering,
pubmed-meshheading:15017387-Saccharomyces cerevisiae,
pubmed-meshheading:15017387-Trans-Activators,
pubmed-meshheading:15017387-Transcription Factors,
pubmed-meshheading:15017387-Two-Hybrid System Techniques
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pubmed:year |
2004
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pubmed:articleTitle |
E2FBP1/hDril1 modulates cell growth through downregulation of promyelocytic leukemia bodies.
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pubmed:affiliation |
Department of Molecular Cellular Oncology and Microbiology, Graduate School, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8549, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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