Statements in which the resource exists as a subject.
PredicateObject
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