| http://purl.uniprot.org/citations/20519433 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20519433 | http://www.w3.org/2000/01/rdf-schema#comment | "Adenomatous polyposis coli (APC), a tumor suppressor commonly mutated in cancer, is a cytoskeletal organizer for cell migration and a scaffold for GSK3 beta/CKI-mediated phosphorylation and degradation of the Wnt effector beta-catenin. It remains unclear whether these different APC functions are coupled, or independently regulated and localized. In primary endothelial cells, we show that GSK3 beta/CKI-phosphorylated APC localizes to microtubule-dependent clusters at the tips of membrane extensions. Loss of GSK3 beta/CKI-phosphorylated APC from these clusters correlates with a decrease in cell migration. GSK3 beta/CKI-phosphorylated APC and beta-catenin at clusters is degraded rapidly by the proteasome, but inhibition of GSK3 beta/CKI does not increase beta-catenin-mediated transcription. GSK3 beta/CKI-phosphorylated and -nonphosphorylated APC also localize along adherens junctions, which requires actin and cell-cell adhesion. Significantly, inhibition of cell-cell adhesion results in loss of lateral membrane APC and a concomitant increase in GSK3 beta/CKI-phosphorylated APC in clusters. These results uncouple different APC functions and show that GSK3 beta/CKI phosphorylation regulates APC clusters and cell migration independently of cell-cell adhesion and beta-catenin transcriptional activity."xsd:string |
| http://purl.uniprot.org/citations/20519433 | http://purl.org/dc/terms/identifier | "doi:10.1091/mbc.e10-03-0235"xsd:string |
| http://purl.uniprot.org/citations/20519433 | http://purl.uniprot.org/core/author | "Nelson W.J."xsd:string |
| http://purl.uniprot.org/citations/20519433 | http://purl.uniprot.org/core/author | "Harris E.S."xsd:string |
| http://purl.uniprot.org/citations/20519433 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20519433 | http://purl.uniprot.org/core/name | "Mol Biol Cell"xsd:string |
| http://purl.uniprot.org/citations/20519433 | http://purl.uniprot.org/core/pages | "2611-2623"xsd:string |
| http://purl.uniprot.org/citations/20519433 | http://purl.uniprot.org/core/title | "Adenomatous polyposis coli regulates endothelial cell migration independent of roles in beta-catenin signaling and cell-cell adhesion."xsd:string |
| http://purl.uniprot.org/citations/20519433 | http://purl.uniprot.org/core/volume | "21"xsd:string |
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