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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2001-7-6
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pubmed:abstractText |
Tissue-specific overexpression of the glycogen synthase kinase-3 (GSK-3) ortholog shaggy (sgg) shortens the period of the Drosophila circadian locomotor activity cycle. The short period phenotype was attributed to premature nuclear translocation of the PERIOD/TIMELESS heterodimer. Reducing SGG/GSK-3 activity lengthens period, demonstrating an intrinsic role for the kinase in circadian rhythmicity. Lowered sgg activity decreased TIMELESS phosphorylation, and it was found that GSK-3 beta specifically phosphorylates TIMELESS in vitro. Overexpression of sgg in vivo converts hypophosphorylated TIMELESS to a hyperphosphorylated protein whose electrophoretic mobility, and light and phosphatase sensitivity, are indistinguishable from the rhythmically produced hyperphosphorylated TIMELESS of wild-type flies. Our results indicate a role for SGG/GSK-3 in TIMELESS phosphorylation and in the regulated nuclear translocation of the PERIOD/TIMELESS heterodimer.
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pubmed:grant |
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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/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycogen Synthase Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PER protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/Period Circadian Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/shaggy protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/timeless protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
105
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
769-79
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11440719-Active Transport, Cell Nucleus,
pubmed-meshheading:11440719-Animals,
pubmed-meshheading:11440719-Biological Clocks,
pubmed-meshheading:11440719-Cell Nucleus,
pubmed-meshheading:11440719-Circadian Rhythm,
pubmed-meshheading:11440719-Dimerization,
pubmed-meshheading:11440719-Drosophila Proteins,
pubmed-meshheading:11440719-Drosophila melanogaster,
pubmed-meshheading:11440719-Glycogen Synthase Kinase 3,
pubmed-meshheading:11440719-Immunoblotting,
pubmed-meshheading:11440719-Insect Proteins,
pubmed-meshheading:11440719-Microscopy, Fluorescence,
pubmed-meshheading:11440719-Motor Activity,
pubmed-meshheading:11440719-Nuclear Proteins,
pubmed-meshheading:11440719-Period Circadian Proteins,
pubmed-meshheading:11440719-Phosphorylation,
pubmed-meshheading:11440719-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11440719-RNA,
pubmed-meshheading:11440719-Recombinant Fusion Proteins
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pubmed:year |
2001
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pubmed:articleTitle |
A role for the segment polarity gene shaggy/GSK-3 in the Drosophila circadian clock.
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pubmed:affiliation |
Laboratory of Genetics and National Science Foundation Science and Technology Center for Biological Timing, The Rockefeller University, New York, NY 10021, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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