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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1999-11-26
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pubmed:abstractText |
In Drosophila, a tendon cell is selected from a group of equipotent precursors following its interaction with a muscle cell. This interaction results in elevated levels of the transcription factor Stripe in the future tendon cells. Here we show that the balance between two distinct forms of the RNA-binding protein How maintains low levels of Stripe at the precursor stage and high levels in the mature tendon. The long, nuclear-specific protein How(L) downregulates Stripe protein levels at the precursor stage by binding stripe mRNA and inhibiting its nuclear export. This inhibition is likely to be counteracted by the short How(S) protein, present in both nucleus and cytoplasm, which is upregulated in the muscle-bound tendon cell following EGF receptor activation.
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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/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/RNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/how protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/stripe protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
573-84
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10549289-Alternative Splicing,
pubmed-meshheading:10549289-Amino Acid Sequence,
pubmed-meshheading:10549289-Animals,
pubmed-meshheading:10549289-Cell Differentiation,
pubmed-meshheading:10549289-DNA-Binding Proteins,
pubmed-meshheading:10549289-Drosophila,
pubmed-meshheading:10549289-Drosophila Proteins,
pubmed-meshheading:10549289-Fluorescent Antibody Technique,
pubmed-meshheading:10549289-Gene Expression Regulation, Developmental,
pubmed-meshheading:10549289-In Situ Hybridization,
pubmed-meshheading:10549289-Molecular Sequence Data,
pubmed-meshheading:10549289-Mutation,
pubmed-meshheading:10549289-Nuclear Proteins,
pubmed-meshheading:10549289-Protein Isoforms,
pubmed-meshheading:10549289-RNA, Messenger,
pubmed-meshheading:10549289-RNA-Binding Proteins,
pubmed-meshheading:10549289-Receptor, Epidermal Growth Factor,
pubmed-meshheading:10549289-Sequence Homology, Amino Acid,
pubmed-meshheading:10549289-Tendons,
pubmed-meshheading:10549289-Transcription Factors,
pubmed-meshheading:10549289-Transfection
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pubmed:year |
1999
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pubmed:articleTitle |
The balance between two isoforms of the Drosophila RNA-binding protein how controls tendon cell differentiation.
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pubmed:affiliation |
Department of Molecular Genetics, Weizmann Institute of Science, Rehovot, Israel.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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