Source:http://linkedlifedata.com/resource/pubmed/id/16778193
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
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pubmed:dateCreated |
2006-6-16
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pubmed:abstractText |
Promyelocytic leukemia (PML) has been implicated in a variety of functions, including control of TP53 function and modulation of cellular senescence. Sumolated PML is the organizer of mature PML bodies, recruiting a variety of proteins onto these nuclear domains. The PML gene is predicted to encode a variety of protein isoforms. Overexpression of only one of them, PML-IV, promotes senescence in human diploid fibroblasts, whereas PML-III was proposed to specifically interact with the centrosome. We show that all PML isoform proteins are expressed in cell lines or primary cells. Unexpectedly, we found that PML-III, PML-IV, and PML-V are quantitatively minor isoforms compared with PML-I/II and could not confirm the centrosomal targeting of PML-III. Stable expression of each isoform, in a pml-null background, yields distinct subcellular localization patterns, suggesting that, like in other RBCC/TRIM proteins, the COOH-terminal domains of PML are involved in interactions with specific cellular components. Only the isoform-specific sequences of PML-I and PML-V are highly conserved between man and mouse. That PML-I contains all conserved exons and is more abundantly expressed than PML-IV suggests that it is a critical contributor to PML function(s).
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PML protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Pml protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0008-5472
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
66
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6192-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:16778193-Animals,
pubmed-meshheading:16778193-COS Cells,
pubmed-meshheading:16778193-Cell Nucleus,
pubmed-meshheading:16778193-Centrosome,
pubmed-meshheading:16778193-Cercopithecus aethiops,
pubmed-meshheading:16778193-HeLa Cells,
pubmed-meshheading:16778193-Humans,
pubmed-meshheading:16778193-Mice,
pubmed-meshheading:16778193-Neoplasm Proteins,
pubmed-meshheading:16778193-Neoplasms,
pubmed-meshheading:16778193-Nuclear Proteins,
pubmed-meshheading:16778193-Protein Isoforms,
pubmed-meshheading:16778193-RNA, Messenger,
pubmed-meshheading:16778193-Transcription Factors,
pubmed-meshheading:16778193-Transfection,
pubmed-meshheading:16778193-Tumor Suppressor Proteins
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pubmed:year |
2006
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pubmed:articleTitle |
Characterization of endogenous human promyelocytic leukemia isoforms.
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pubmed:affiliation |
Centre National de la Recherche Scientifique UMR7151, Equipe Labellisée par La Ligne Contre le Cancer, Paris Cedex, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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