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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5427
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pubmed:dateCreated |
1999-8-12
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pubmed:abstractText |
Most organisms have circadian clocks consisting of negative feedback loops of gene regulation that facilitate adaptation to cycles of light and darkness. In this study, CRYPTOCHROME (CRY), a protein involved in circadian photoperception in Drosophila, is shown to block the function of PERIOD/TIMELESS (PER/TIM) heterodimeric complexes in a light-dependent fashion. TIM degradation does not occur under these conditions; thus, TIM degradation is uncoupled from abrogation of its function by light. CRY and TIM are part of the same complex and directly interact in yeast in a light-dependent fashion. PER/TIM and CRY influence the subcellular distribution of these protein complexes, which reside primarily in the nucleus after the perception of a light signal. Thus, CRY acts as a circadian photoreceptor by directly interacting with core components of the circadian clock.
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pubmed:grant |
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pubmed:commentsCorrections |
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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/Cryptochromes,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Eye Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Flavoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Insect Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent 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/Receptors, G-Protein-Coupled,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/cryptochrome protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/timeless protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
285
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
553-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10417378-Animals,
pubmed-meshheading:10417378-Biological Clocks,
pubmed-meshheading:10417378-Cell Line,
pubmed-meshheading:10417378-Cell Nucleus,
pubmed-meshheading:10417378-Circadian Rhythm,
pubmed-meshheading:10417378-Cryptochromes,
pubmed-meshheading:10417378-Cytoplasm,
pubmed-meshheading:10417378-Darkness,
pubmed-meshheading:10417378-Dimerization,
pubmed-meshheading:10417378-Drosophila,
pubmed-meshheading:10417378-Drosophila Proteins,
pubmed-meshheading:10417378-Eye Proteins,
pubmed-meshheading:10417378-Flavoproteins,
pubmed-meshheading:10417378-Green Fluorescent Proteins,
pubmed-meshheading:10417378-Insect Proteins,
pubmed-meshheading:10417378-Light,
pubmed-meshheading:10417378-Luminescent Proteins,
pubmed-meshheading:10417378-Mutation,
pubmed-meshheading:10417378-Nuclear Proteins,
pubmed-meshheading:10417378-Period Circadian Proteins,
pubmed-meshheading:10417378-Photoreceptor Cells, Invertebrate,
pubmed-meshheading:10417378-Receptors, G-Protein-Coupled,
pubmed-meshheading:10417378-Recombinant Fusion Proteins,
pubmed-meshheading:10417378-Transfection,
pubmed-meshheading:10417378-Yeasts
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pubmed:year |
1999
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pubmed:articleTitle |
Light-dependent sequestration of TIMELESS by CRYPTOCHROME.
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pubmed:affiliation |
Department of Cell Biology and NSF Center for Biological Timing, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, 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.,
Research Support, Non-U.S. Gov't
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