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http://purl.uniprot.org/citations/17190795http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17190795http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17190795http://www.w3.org/2000/01/rdf-schema#comment"The tensin family member cten (C-terminal tensin like) is an Src homology 2 (SH2) and phosphotyrosine binding domain-containing focal adhesion molecule that may function as a tumor suppressor. However, the mechanism has not been well established. We report that cten binds to another tumor suppressor, deleted in liver cancer 1 (DLC-1), and the SH2 domain of cten is responsible for the interaction. Unexpectedly, the interaction between DLC-1 and the cten SH2 domain is independent of tyrosine phosphorylation of DLC-1. By site-directed mutagenesis, we have identified several amino acid residues on cten and DLC-1 that are essential for this interaction. Mutations on DLC-1 perturb the interaction with cten and disrupt the focal adhesion localization of DLC-1. Furthermore, these DLC-1 mutants have lost their tumor suppression activities. When these DLC-1 mutants were fused to a focal adhesion targeting sequence, their tumor suppression activities were significantly restored. These results provide a novel mechanism whereby the SH2 domain of cten-mediated focal adhesion localization of DLC-1 plays an essential role in its tumor suppression activity."xsd:string
http://purl.uniprot.org/citations/17190795http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200608015"xsd:string
http://purl.uniprot.org/citations/17190795http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200608015"xsd:string
http://purl.uniprot.org/citations/17190795http://purl.uniprot.org/core/author"deVere White R.W."xsd:string
http://purl.uniprot.org/citations/17190795http://purl.uniprot.org/core/author"deVere White R.W."xsd:string
http://purl.uniprot.org/citations/17190795http://purl.uniprot.org/core/author"Si L."xsd:string
http://purl.uniprot.org/citations/17190795http://purl.uniprot.org/core/author"Si L."xsd:string
http://purl.uniprot.org/citations/17190795http://purl.uniprot.org/core/author"Lo S.H."xsd:string
http://purl.uniprot.org/citations/17190795http://purl.uniprot.org/core/author"Lo S.H."xsd:string
http://purl.uniprot.org/citations/17190795http://purl.uniprot.org/core/author"Liao Y.C."xsd:string
http://purl.uniprot.org/citations/17190795http://purl.uniprot.org/core/author"Liao Y.C."xsd:string
http://purl.uniprot.org/citations/17190795http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17190795http://purl.uniprot.org/core/date"2007"xsd:gYear
http://purl.uniprot.org/citations/17190795http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/17190795http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/17190795http://purl.uniprot.org/core/pages"43-49"xsd:string
http://purl.uniprot.org/citations/17190795http://purl.uniprot.org/core/pages"43-49"xsd:string
http://purl.uniprot.org/citations/17190795http://purl.uniprot.org/core/title"The phosphotyrosine-independent interaction of DLC-1 and the SH2 domain of cten regulates focal adhesion localization and growth suppression activity of DLC-1."xsd:string
http://purl.uniprot.org/citations/17190795http://purl.uniprot.org/core/title"The phosphotyrosine-independent interaction of DLC-1 and the SH2 domain of cten regulates focal adhesion localization and growth suppression activity of DLC-1."xsd:string
http://purl.uniprot.org/citations/17190795http://purl.uniprot.org/core/volume"176"xsd:string
http://purl.uniprot.org/citations/17190795http://purl.uniprot.org/core/volume"176"xsd:string
http://purl.uniprot.org/citations/17190795http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17190795
http://purl.uniprot.org/citations/17190795http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/17190795