Source:http://linkedlifedata.com/resource/pubmed/id/14996909
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 8
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pubmed:dateCreated |
2004-3-15
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pubmed:abstractText |
Nucleocytoplasmic transport of proteins plays an important role in the regulation of many cellular processes. Differences in nucleocytoplasmic shuttling can provide a basis for isoform-specific biological functions for members of multigene families, like the 14-3-3 protein family. Many organisms contain multiple 14-3-3 isoforms, which play a role in numerous processes, including signalling, cell cycle control and apoptosis. It is still unclear whether these isoforms have specialised biological functions and whether this specialisation is based on isoform-specific ligand binding, expression regulation or specific localisation. Therefore, we studied the subcellular distribution of 14-3-3 sigma and 14-3-3 zeta in vivo in various mammalian cell types using yellow fluorescent protein fusions and isoform-specific antibodies. 14-3-3 sigma was mainly localised in the cytoplasm and only low levels were present in the nucleus, whereas 14-3-3 zeta was found at relatively higher levels in the nucleus. Fluorescence recovery after photobleaching (FRAP) experiments indicated that the 14-3-3 proteins rapidly shuttle in and out of the nucleus through active transport and that the distinct subcellular distributions of 14-3-3 sigma and 14-3-3 zeta are caused by differences in nuclear export. 14-3-3 sigma had a 1.7x higher nuclear export rate constant than 14-3-3 zeta, while import rate constants were equal. The 14-3-3 proteins are exported from the nucleus at least in part by a Crm1-dependent, leptomycin B-sensitive mechanism. The differences in subcellular distribution of 14-3-3 that we found in this study are likely to reflect a molecular basis for isoform-specific biological specialisation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0021-9533
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
117
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1411-20
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pubmed:meshHeading |
pubmed-meshheading:14996909-14-3-3 Proteins,
pubmed-meshheading:14996909-Blotting, Western,
pubmed-meshheading:14996909-Cell Line,
pubmed-meshheading:14996909-Cell Nucleus,
pubmed-meshheading:14996909-Cytoplasm,
pubmed-meshheading:14996909-Fluorescence Recovery After Photobleaching,
pubmed-meshheading:14996909-Fluorescent Antibody Technique, Indirect,
pubmed-meshheading:14996909-Fluorescent Dyes,
pubmed-meshheading:14996909-HeLa Cells,
pubmed-meshheading:14996909-Humans,
pubmed-meshheading:14996909-Kinetics,
pubmed-meshheading:14996909-Protein Isoforms,
pubmed-meshheading:14996909-Protein Transport,
pubmed-meshheading:14996909-Recombinant Fusion Proteins,
pubmed-meshheading:14996909-Subcellular Fractions
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pubmed:year |
2004
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pubmed:articleTitle |
Isoform-specific differences in rapid nucleocytoplasmic shuttling cause distinct subcellular distributions of 14-3-3 sigma and 14-3-3 zeta.
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pubmed:affiliation |
Section Molecular Cell Biology, Institute of Biology, Leiden University, Wassenaarseweg 64, 2333 AL Leiden, The Netherlands. hermert@rulbim.leidenuniv.nl
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pubmed:publicationType |
Journal Article
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