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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 |
2002-4-16
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pubmed:abstractText |
The secreted signaling molecule Hedgehog regulates gene expression in target cells in part by preventing proteolysis of the full-length Cubitus interruptus (Ci-155) transcriptional activator to the Ci-75 repressor form. Ci-155 proteolysis depends on phosphorylation at three sites by Protein Kinase A (PKA). We show that these phosphoserines prime further phosphorylation at adjacent Glycogen Synthase Kinase 3 (GSK3) and Casein Kinase I (CK1) sites. Alteration of the GSK3 or CK1 sites prevents Ci-155 proteolysis and activates Ci in the absence of Hedgehog. Ci-155 proteolysis is also inhibited if cells lack activity of the Drosophila GSK3, Shaggy, previously implicated in Wingless signaling. Conversely, Ci-155 levels are reduced in Hedgehog-responding cells by overexpression of PKA and the Drosophila CK1, Double-time, a regulator of circadian rhythms.
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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/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Casein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclic AMP-Dependent Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycogen Synthase Kinase 3,
http://linkedlifedata.com/resource/pubmed/chemical/Glycogen Synthase Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Hedgehog Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Wnt Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Zebrafish Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ci protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/hedgehog protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/shaggy protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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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 |
22
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pubmed:volume |
108
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
823-35
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11955435-Amino Acid Sequence,
pubmed-meshheading:11955435-Animals,
pubmed-meshheading:11955435-Binding Sites,
pubmed-meshheading:11955435-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:11955435-Casein Kinases,
pubmed-meshheading:11955435-Cyclic AMP-Dependent Protein Kinases,
pubmed-meshheading:11955435-DNA-Binding Proteins,
pubmed-meshheading:11955435-Drosophila,
pubmed-meshheading:11955435-Drosophila Proteins,
pubmed-meshheading:11955435-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:11955435-Glycogen Synthase Kinase 3,
pubmed-meshheading:11955435-Glycogen Synthase Kinases,
pubmed-meshheading:11955435-Hedgehog Proteins,
pubmed-meshheading:11955435-Molecular Sequence Data,
pubmed-meshheading:11955435-Mutation,
pubmed-meshheading:11955435-Phosphorylation,
pubmed-meshheading:11955435-Protein Kinases,
pubmed-meshheading:11955435-Protein-Serine-Threonine Kinases,
pubmed-meshheading:11955435-Proto-Oncogene Proteins,
pubmed-meshheading:11955435-Signal Transduction,
pubmed-meshheading:11955435-Transcription Factors,
pubmed-meshheading:11955435-Wnt Proteins,
pubmed-meshheading:11955435-Zebrafish Proteins
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pubmed:year |
2002
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pubmed:articleTitle |
Proteolysis of the Hedgehog signaling effector Cubitus interruptus requires phosphorylation by Glycogen Synthase Kinase 3 and Casein Kinase 1.
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pubmed:affiliation |
Department of Biological Sciences, Columbia University, New York, NY 10027, USA.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.
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