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http://purl.uniprot.org/citations/11976333http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11976333http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11976333http://www.w3.org/2000/01/rdf-schema#comment"Cadherins function to promote adhesion between adjacent cells and play critical roles in such cellular processes as development, tissue maintenance, and tumor suppression. We previously demonstrated that heterotrimeric G proteins of the G12 subfamily comprised of Galpha12 and Galpha13 interact with the cytoplasmic domain of cadherins and cause the release of the transcriptional activator beta-catenin (Meigs, T. E., Fields, T. A., McKee, D. D., and Casey, P. J. (2001) Proc. Natl. Acad. Sci. U. S. A. 98, 519-524). Because of the importance of beta-catenin in cadherin-mediated cell-cell adhesion, we examined whether G12 subfamily proteins could also regulate cadherin function. The introduction of mutationally activated G12 proteins into K562 cells expressing E-cadherin blocked cadherin-mediated cell adhesion in steady-state assays. Also, in breast cancer cells, the introduction of activated G12 proteins blocked E-cadherin function in a fast aggregation assay. Aggregation mediated by a mutant cadherin that lacks G12 binding ability was not affected by activated G12 proteins, indicating a requirement for direct G12-cadherin interaction. Furthermore, in wound-filling assays in which ectopic expression of E-cadherin inhibits cell migration, the expression of activated G12 proteins reversed the inhibition via a mechanism that was independent of G12-mediated Rho activation. These results validate the G12-cadherin interaction as a potentially important event in cell biology and suggest novel roles for G12 proteins in the regulation of cadherin-mediated developmental events and in the loss of cadherin function that is characteristic of metastatic tumor progression."xsd:string
http://purl.uniprot.org/citations/11976333http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m201984200"xsd:string
http://purl.uniprot.org/citations/11976333http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m201984200"xsd:string
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/author"Meigs T.E."xsd:string
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/author"Meigs T.E."xsd:string
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/author"Casey P.J."xsd:string
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/author"Casey P.J."xsd:string
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/author"Fedor-Chaiken M."xsd:string
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/author"Fedor-Chaiken M."xsd:string
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/author"Brackenbury R."xsd:string
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/author"Brackenbury R."xsd:string
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/author"Kaplan D.D."xsd:string
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/author"Kaplan D.D."xsd:string
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/pages"24594-24600"xsd:string
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/pages"24594-24600"xsd:string
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/title"Galpha12 and Galpha13 negatively regulate the adhesive functions of cadherin."xsd:string
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/title"Galpha12 and Galpha13 negatively regulate the adhesive functions of cadherin."xsd:string
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/volume"277"xsd:string
http://purl.uniprot.org/citations/11976333http://purl.uniprot.org/core/volume"277"xsd:string