Source:http://linkedlifedata.com/resource/pubmed/id/16357871
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
7076
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pubmed:dateCreated |
2006-2-2
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pubmed:abstractText |
How a cell chooses to proliferate or to differentiate is an important issue in stem cell and cancer biology. Drosophila neuroblasts undergo self-renewal with every cell division, producing another neuroblast and a differentiating daughter cell, but the mechanisms controlling the self-renewal/differentiation decision are poorly understood. Here we tested whether cell polarity genes, known to regulate embryonic neuroblast asymmetric cell division, also regulate neuroblast self-renewal. Clonal analysis in larval brains showed that pins mutant neuroblasts rapidly fail to self-renew, whereas lethal giant larvae (lgl) mutant neuroblasts generate multiple neuroblasts. Notably, lgl pins double mutant neuroblasts all divide symmetrically to self-renew, filling the brain with neuroblasts at the expense of neurons. The lgl pins neuroblasts show ectopic cortical localization of atypical protein kinase C (aPKC), and a decrease in aPKC expression reduces neuroblast numbers, suggesting that aPKC promotes neuroblast self-renewal. In support of this hypothesis, neuroblast-specific overexpression of membrane-targeted aPKC, but not a kinase-dead version, induces ectopic neuroblast self-renewal. We conclude that cortical aPKC kinase activity is a potent inducer of neuroblast self-renewal.
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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/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotide Dissociation...,
http://linkedlifedata.com/resource/pubmed/chemical/PKC-3 protein,
http://linkedlifedata.com/resource/pubmed/chemical/Pins protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Tumor Suppressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/lethal (2) giant larvae protein...
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
1476-4687
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
2
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pubmed:volume |
439
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
594-8
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:16357871-Animals,
pubmed-meshheading:16357871-Cell Differentiation,
pubmed-meshheading:16357871-Cell Division,
pubmed-meshheading:16357871-Cell Polarity,
pubmed-meshheading:16357871-Drosophila Proteins,
pubmed-meshheading:16357871-Drosophila melanogaster,
pubmed-meshheading:16357871-Guanine Nucleotide Dissociation Inhibitors,
pubmed-meshheading:16357871-Larva,
pubmed-meshheading:16357871-Mutation,
pubmed-meshheading:16357871-Neurons,
pubmed-meshheading:16357871-Protein Kinase C,
pubmed-meshheading:16357871-Tumor Suppressor Proteins
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pubmed:year |
2006
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pubmed:articleTitle |
Lgl, Pins and aPKC regulate neuroblast self-renewal versus differentiation.
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pubmed:affiliation |
Institutes of Neuroscience and Molecular Biology, Howard Hughes Medical Institute, University of Oregon 1254, Eugene, Oregon 97403, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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