rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
5410
|
pubmed:dateCreated |
1999-4-15
|
pubmed:abstractText |
Dysregulation of Wnt-beta-catenin signaling disrupts axis formation in vertebrate embryos and underlies multiple human malignancies. The adenomatous polyposis coli (APC) protein, axin, and glycogen synthase kinase 3beta form a Wnt-regulated signaling complex that mediates the phosphorylation-dependent degradation of beta-catenin. A protein phosphatase 2A (PP2A) regulatory subunit, B56, interacted with APC in the yeast two-hybrid system. Expression of B56 reduced the abundance of beta-catenin and inhibited transcription of beta-catenin target genes in mammalian cells and Xenopus embryo explants. The B56-dependent decrease in beta-catenin was blocked by oncogenic mutations in beta-catenin or APC, and by proteasome inhibitors. B56 may direct PP2A to dephosphorylate specific components of the APC-dependent signaling complex and thereby inhibit Wnt signaling.
|
pubmed:grant |
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenomatous Polyposis Coli Protein,
http://linkedlifedata.com/resource/pubmed/chemical/CTNNB1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Calmodulin-Dependent...,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Proteinase Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal 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/Leupeptins,
http://linkedlifedata.com/resource/pubmed/chemical/Multienzyme Complexes,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Trans-Activators,
http://linkedlifedata.com/resource/pubmed/chemical/Wnt Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Xenopus Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Zebrafish Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/acetylleucyl-leucyl-norleucinal,
http://linkedlifedata.com/resource/pubmed/chemical/benzyloxycarbonylleucyl-leucyl-leuci...,
http://linkedlifedata.com/resource/pubmed/chemical/beta Catenin,
http://linkedlifedata.com/resource/pubmed/chemical/beta-catenin protein, Xenopus
|
pubmed:status |
MEDLINE
|
pubmed:month |
Mar
|
pubmed:issn |
0036-8075
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
26
|
pubmed:volume |
283
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
2089-91
|
pubmed:dateRevised |
2009-11-19
|
pubmed:meshHeading |
pubmed-meshheading:10092233-Adenomatous Polyposis Coli Protein,
pubmed-meshheading:10092233-Animals,
pubmed-meshheading:10092233-Calcium-Calmodulin-Dependent Protein Kinases,
pubmed-meshheading:10092233-Cell Line,
pubmed-meshheading:10092233-Cysteine Endopeptidases,
pubmed-meshheading:10092233-Cysteine Proteinase Inhibitors,
pubmed-meshheading:10092233-Cytoskeletal Proteins,
pubmed-meshheading:10092233-Down-Regulation,
pubmed-meshheading:10092233-Genes, Reporter,
pubmed-meshheading:10092233-Glycogen Synthase Kinase 3,
pubmed-meshheading:10092233-Glycogen Synthase Kinases,
pubmed-meshheading:10092233-Humans,
pubmed-meshheading:10092233-Leupeptins,
pubmed-meshheading:10092233-Multienzyme Complexes,
pubmed-meshheading:10092233-Mutation,
pubmed-meshheading:10092233-Phosphoprotein Phosphatases,
pubmed-meshheading:10092233-Phosphorylation,
pubmed-meshheading:10092233-Proteasome Endopeptidase Complex,
pubmed-meshheading:10092233-Protein Phosphatase 2,
pubmed-meshheading:10092233-Proto-Oncogene Proteins,
pubmed-meshheading:10092233-Signal Transduction,
pubmed-meshheading:10092233-Trans-Activators,
pubmed-meshheading:10092233-Transcriptional Activation,
pubmed-meshheading:10092233-Transfection,
pubmed-meshheading:10092233-Tumor Cells, Cultured,
pubmed-meshheading:10092233-Wnt Proteins,
pubmed-meshheading:10092233-Xenopus,
pubmed-meshheading:10092233-Xenopus Proteins,
pubmed-meshheading:10092233-Zebrafish Proteins,
pubmed-meshheading:10092233-beta Catenin
|
pubmed:year |
1999
|
pubmed:articleTitle |
Regulation of beta-catenin signaling by the B56 subunit of protein phosphatase 2A.
|
pubmed:affiliation |
Department of Oncological Sciences, Huntsman Cancer Institute, University of Utah, Salt Lake City, UT 84132, USA.
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|