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http://purl.uniprot.org/citations/19941816http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19941816http://www.w3.org/2000/01/rdf-schema#comment"Increased transcriptional activity of beta-catenin resulting from Wnt/Wingless-dependent or -independent signaling has been detected in many types of human cancer, but the underlying mechanism of Wnt-independent regulation remains unclear. We demonstrate here that EGFR activation results in disruption of the complex of beta-catenin and alpha-catenin, thereby abrogating the inhibitory effect of alpha-catenin on beta-catenin transactivation via CK2alpha-dependent phosphorylation of alpha-catenin at S641. ERK2, which is activated by EGFR signaling, directly binds to CK2alpha via the ERK2 docking groove and phosphorylates CK2alpha primarily at T360/S362, subsequently enhancing CK2alpha activity toward alpha-catenin phosphorylation. In addition, levels of alpha-catenin S641 phosphorylation correlate with levels of ERK1/2 activity in human glioblastoma specimens and with grades of glioma malignancy. This EGFR-ERK-CK2-mediated phosphorylation of alpha-catenin promotes beta-catenin transactivation and tumor cell invasion. These findings highlight the importance of the crosstalk between EGFR and Wnt pathways in tumor development."xsd:string
http://purl.uniprot.org/citations/19941816http://purl.org/dc/terms/identifier"doi:10.1016/j.molcel.2009.09.034"xsd:string
http://purl.uniprot.org/citations/19941816http://purl.uniprot.org/core/author"Lu Z."xsd:string
http://purl.uniprot.org/citations/19941816http://purl.uniprot.org/core/author"Wang J."xsd:string
http://purl.uniprot.org/citations/19941816http://purl.uniprot.org/core/author"Hawke D."xsd:string
http://purl.uniprot.org/citations/19941816http://purl.uniprot.org/core/author"Fang X."xsd:string
http://purl.uniprot.org/citations/19941816http://purl.uniprot.org/core/author"Ji H."xsd:string
http://purl.uniprot.org/citations/19941816http://purl.uniprot.org/core/author"Fang D."xsd:string
http://purl.uniprot.org/citations/19941816http://purl.uniprot.org/core/author"Fang B."xsd:string
http://purl.uniprot.org/citations/19941816http://purl.uniprot.org/core/author"Aldape K."xsd:string
http://purl.uniprot.org/citations/19941816http://purl.uniprot.org/core/author"Ge Q."xsd:string
http://purl.uniprot.org/citations/19941816http://purl.uniprot.org/core/author"Litchfield D.W."xsd:string
http://purl.uniprot.org/citations/19941816http://purl.uniprot.org/core/author"Keezer S."xsd:string
http://purl.uniprot.org/citations/19941816http://purl.uniprot.org/core/author"Nika H."xsd:string
http://purl.uniprot.org/citations/19941816http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19941816http://purl.uniprot.org/core/name"Mol Cell"xsd:string
http://purl.uniprot.org/citations/19941816http://purl.uniprot.org/core/pages"547-559"xsd:string
http://purl.uniprot.org/citations/19941816http://purl.uniprot.org/core/title"EGF-induced ERK activation promotes CK2-mediated disassociation of alpha-Catenin from beta-Catenin and transactivation of beta-Catenin."xsd:string
http://purl.uniprot.org/citations/19941816http://purl.uniprot.org/core/volume"36"xsd:string
http://purl.uniprot.org/citations/19941816http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19941816
http://purl.uniprot.org/citations/19941816http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19941816
http://purl.uniprot.org/uniprot/#_A0A384MDY0-mappedCitation-19941816http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19941816
http://purl.uniprot.org/uniprot/#_B3KSR8-mappedCitation-19941816http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19941816
http://purl.uniprot.org/uniprot/#_B4DSW9-mappedCitation-19941816http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19941816