Source:http://linkedlifedata.com/resource/pubmed/id/20876583
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
48
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pubmed:dateCreated |
2010-11-24
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pubmed:abstractText |
Casein kinase 2 (CK2) is a typical serine/threonine kinase consisting of ? and ? subunits and has been implicated in many cellular and developmental processes. In this study, we demonstrate that CK2 is a positive regulator of the Hedgehog (Hh) signal transduction pathway. We found that inactivation of CK2 by CK2? RNAi enhances the loss-of-Hh wing phenotype induced by a dominant negative form of Smoothened (Smo). CK2? RNAi attenuates Hh-induced Smo accumulation and down-regulates Hh target gene expression, whereas increasing CK2 activity by coexpressing CK2? and CK2? increases Smo accumulation and induces ectopic Hh target gene expression. We identified the serine residues in Smo that can be phosphorylated by CK2 in vitro. Mutating these serine residues attenuates the ability of Smo to transduce high level Hh signaling activity in vivo. Furthermore, we found that CK2 plays an additional positive role downstream of Smo by regulating the stability of full-length Cubitus interruptus (Ci). CK2? RNAi promotes Ci degradation whereas coexpressing CK2? and CK2? increases the half-life of Ci. We showed that CK2 prevents Ci ubiquitination and degradation by the proteasome. Thus, CK2 promotes Hh signaling activity by regulating multiple pathway components.
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pubmed:grant |
http://linkedlifedata.com/resource/pubmed/grant/GM061269,
http://linkedlifedata.com/resource/pubmed/grant/GM067045,
http://linkedlifedata.com/resource/pubmed/grant/GM079684,
http://linkedlifedata.com/resource/pubmed/grant/R01 GM079684-03,
http://linkedlifedata.com/resource/pubmed/grant/R01 GM079684-04
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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/Casein Kinase II,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Drosophila Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hedgehog Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, G-Protein-Coupled,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/ci protein, Drosophila,
http://linkedlifedata.com/resource/pubmed/chemical/smoothened protein, Drosophila
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1083-351X
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
26
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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 |
37218-26
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pubmed:dateRevised |
2011-5-3
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pubmed:meshHeading |
pubmed-meshheading:20876583-Animals,
pubmed-meshheading:20876583-Casein Kinase II,
pubmed-meshheading:20876583-DNA-Binding Proteins,
pubmed-meshheading:20876583-Drosophila Proteins,
pubmed-meshheading:20876583-Drosophila melanogaster,
pubmed-meshheading:20876583-Gene Expression Regulation,
pubmed-meshheading:20876583-Hedgehog Proteins,
pubmed-meshheading:20876583-Protein Stability,
pubmed-meshheading:20876583-Receptors, G-Protein-Coupled,
pubmed-meshheading:20876583-Signal Transduction,
pubmed-meshheading:20876583-Transcription Factors
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pubmed:year |
2010
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pubmed:articleTitle |
Casein kinase 2 promotes Hedgehog signaling by regulating both smoothened and Cubitus interruptus.
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pubmed:affiliation |
Department of Molecular and Cellular Biochemistry, Markey Cancer Center, University of Kentucky, Lexington, Kentucky 40536, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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