Source:http://linkedlifedata.com/resource/pubmed/id/12878198
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
4
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pubmed:dateCreated |
2003-7-24
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pubmed:abstractText |
Posttranslational modification plays important roles in a range of cellular functions. Poly(ADP-ribosyl)ation influences DNA repair, transcription, centrosome duplication, and chromosome stability. Poly(ADP-ribose) attached to acceptor proteins should be properly hydrolyzed by poly(ADP-ribose) glycohydrolase (PARG). However the subcellular localization and the role of PARG have not been well characterized. Here, we transiently expressed GFP- or Myc-tagged human PARG in mammalian cells and revealed that the subcellular distribution of human PARG changes dramatically during the cell cycle. GFP-hPARG is found almost exclusively in the nucleus during interphase. During mitosis, most GFP-hPARG protein localizes to the cytoplasm and hardly any GFP-hPARG protein is found associated with the chromosomes. Furthermore, we found that GFP-hPARG localizes to the centrosomes during mitosis. Our findings suggest that shuttling of PARG between nucleus and cytoplasm and proper control of poly(ADP-ribose) metabolism throughout the cell cycle may play an important role in regulating cell cycle progression and centrosome duplication.
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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/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/poly ADP-ribose glycohydrolase
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-291X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
307
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
915-21
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12878198-3T3 Cells,
pubmed-meshheading:12878198-Animals,
pubmed-meshheading:12878198-COS Cells,
pubmed-meshheading:12878198-Cell Cycle,
pubmed-meshheading:12878198-Cell Nucleus,
pubmed-meshheading:12878198-Centrosome,
pubmed-meshheading:12878198-Cytoplasm,
pubmed-meshheading:12878198-Genetic Vectors,
pubmed-meshheading:12878198-Glycoside Hydrolases,
pubmed-meshheading:12878198-Green Fluorescent Proteins,
pubmed-meshheading:12878198-Humans,
pubmed-meshheading:12878198-Luminescent Proteins,
pubmed-meshheading:12878198-Mice,
pubmed-meshheading:12878198-Recombinant Fusion Proteins,
pubmed-meshheading:12878198-Tumor Cells, Cultured
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pubmed:year |
2003
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pubmed:articleTitle |
Subcellular localization of poly(ADP-ribose) glycohydrolase in mammalian cells.
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pubmed:affiliation |
Department of Biochemistry and Molecular Oncology, Institute of Basic Medical Sciences, University of Tsukuba, 1-1-1, Tennoudai, Tsukuba Science City, Ibaraki 305-8575, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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