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http://purl.uniprot.org/citations/10838081http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10838081http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10838081http://www.w3.org/2000/01/rdf-schema#comment"Hic-5 is a CAKbeta-binding protein localized at focal adhesions. Here we show that overexpression of CAKbeta or Fyn, but not FAK, enhanced the tyrosine phosphorylation of coexpressed Hic-5 in COS-7 cells. These phosphorylations were further augmented by stimulating cells with osmotic stress. The Y60F mutant of Hic-5 was not phosphorylated, and Hic-5 phosphorylated on tyrosine 60 was bound specifically to the SH2 domain of Csk. Coexpression experiments revealed that the phosphorylation of Hic-5 by CAKbeta required the kinase activation of CAKbeta and binding of Hic-5 by CAKbeta. Specific phosphorylation of Hic-5 by CAKbeta and Fyn may activate a signaling pathway mediated by Hic-5."xsd:string
http://purl.uniprot.org/citations/10838081http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(00)01597-0"xsd:string
http://purl.uniprot.org/citations/10838081http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(00)01597-0"xsd:string
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/author"Sasaki T."xsd:string
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/author"Sasaki T."xsd:string
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/author"Suzuki R."xsd:string
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/author"Suzuki R."xsd:string
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/author"Ishino M."xsd:string
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/author"Ishino M."xsd:string
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/author"Aoto H."xsd:string
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/author"Aoto H."xsd:string
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/author"Sasaski H."xsd:string
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/author"Sasaski H."xsd:string
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/pages"179-183"xsd:string
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/pages"179-183"xsd:string
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/title"Phosphorylation of Hic-5 at tyrosine 60 by CAKbeta and Fyn."xsd:string
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/title"Phosphorylation of Hic-5 at tyrosine 60 by CAKbeta and Fyn."xsd:string
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/volume"474"xsd:string
http://purl.uniprot.org/citations/10838081http://purl.uniprot.org/core/volume"474"xsd:string