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All rights reserved. http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/dc/elements/1.1/title BEL Framework Large Corpus Document http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/authoredBy http://www.tkuhn.ch/bel2nanopub/RAhGx6RzPtvmCSWD-smof1bk0w23UxIllvL8_TV-y_wi0#_7 http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://purl.org/pav/version 20131211 http://www.tkuhn.ch/bel2nanopub/RAhGx6RzPtvmCSWD-smof1bk0w23UxIllvL8_TV-y_wi0#_6 http://www.w3.org/ns/prov#value Beta-catenin is a transcriptional activator that is regulated by glycogen synthase kinase-3 (GSK-3). GSK-3 is constitutively active in unstimulated cells where it phosphorylates beta-catenin, targeting beta-catenin for rapid degradation. Receptor-induced inhibition of GSK-3 allows beta-catenin to accumulate in the cytoplasm and then translocate to the nucleus where it promotes the transcription of genes such as c-myc and cyclin D1. Wnt hormones, the best known regulators of beta-catenin, inhibit GSK-3 via the Disheveled protein. However, GSK-3 is also inhibited when it is phosphorylated by Akt, a downstream target of phosphatidylinositol 3-kinase (PI3K). We have previously shown that B cell Ag receptor (BCR) signaling leads to activation of PI3K and Akt as well as inhibition of GSK-3. Therefore, we hypothesized that BCR engagement would induce the accumulation of beta-catenin via a PI3K/Akt/GSK-3 pathway. We now show that BCR ligation causes an increase in the level of beta-catenin in the nuclear fraction of B cells as well as an increase in beta-catenin-dependent transcription. Direct inhibition of GSK-3 by LiCl also increased beta-catenin levels in B cells. This suggests that GSK-3 keeps beta-catenin levels low in unstimulated B cells and that BCR-induced inhibition of GSK-3 allows the accumulation of beta-catenin. Surprisingly, we found that the BCR-induced phosphorylation of GSK-3 on its negative regulatory sites, as well as the subsequent up-regulation of beta-catenin, was not mediated by Akt but by the phospholipase C-dependent activation of protein kinase C. Thus, the BCR regulates beta-catenin levels via a phospholipase C/protein kinase C/GSK-3 pathway. http://www.tkuhn.ch/bel2nanopub/RAhGx6RzPtvmCSWD-smof1bk0w23UxIllvL8_TV-y_wi0#_6 http://www.w3.org/ns/prov#wasQuotedFrom http://www.ncbi.nlm.nih.gov/pubmed/12097378 http://www.tkuhn.ch/bel2nanopub/RAhGx6RzPtvmCSWD-smof1bk0w23UxIllvL8_TV-y_wi0#_7 http://www.w3.org/2000/01/rdf-schema#label Selventa http://www.tkuhn.ch/bel2nanopub/RAhGx6RzPtvmCSWD-smof1bk0w23UxIllvL8_TV-y_wi0#assertion http://www.w3.org/ns/prov#hadPrimarySource http://www.ncbi.nlm.nih.gov/pubmed/12097378 http://www.tkuhn.ch/bel2nanopub/RAhGx6RzPtvmCSWD-smof1bk0w23UxIllvL8_TV-y_wi0#assertion http://www.w3.org/ns/prov#wasDerivedFrom http://resource.belframework.org/belframework/20131211/knowledge/large_corpus.bel http://www.tkuhn.ch/bel2nanopub/RAhGx6RzPtvmCSWD-smof1bk0w23UxIllvL8_TV-y_wi0#assertion http://www.w3.org/ns/prov#wasDerivedFrom http://www.tkuhn.ch/bel2nanopub/RAhGx6RzPtvmCSWD-smof1bk0w23UxIllvL8_TV-y_wi0#_6 http://www.tkuhn.ch/bel2nanopub/RAhGx6RzPtvmCSWD-smof1bk0w23UxIllvL8_TV-y_wi0#pubinfo http://www.tkuhn.ch/bel2nanopub/RAhGx6RzPtvmCSWD-smof1bk0w23UxIllvL8_TV-y_wi0 http://purl.org/dc/terms/created 2014-07-03T14:31:51.374+02:00 http://www.tkuhn.ch/bel2nanopub/RAhGx6RzPtvmCSWD-smof1bk0w23UxIllvL8_TV-y_wi0 http://purl.org/pav/createdBy http://orcid.org/0000-0001-6818-334X http://www.tkuhn.ch/bel2nanopub/RAhGx6RzPtvmCSWD-smof1bk0w23UxIllvL8_TV-y_wi0 http://purl.org/pav/createdBy http://orcid.org/0000-0002-1267-0234