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http://purl.uniprot.org/citations/11684708http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11684708http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11684708http://www.w3.org/2000/01/rdf-schema#comment"Keratin 8 and 18 (K8/18) are the major components of intermediate filament (IF) proteins of simple or single-layered epithelia. Recent data show that normal and malignant epithelial cells deficient in K8/18 are nearly 100 times more sensitive to tumor necrosis factor (TNF)-induced cell death. We have now identified human TNF receptor type 1 (TNFR1)-associated death domain protein (TRADD) to be the K18-interacting protein. Among IF proteins tested in two-hybrid systems, TRADD specifically bound K18 and K14, type I (acidic) keratins. The COOH-terminal region of TRADD interacted with the coil Ia of the rod domain of K18. Endogenous TRADD coimmunoprecipitated with K18, and colocalized with K8/18 filaments in human mammary epithelial cells. Overexpression of the NH2 terminus (amino acids 1-270) of K18 containing the TRADD-binding domain as well as overexpression of K8/18 in SW13 cells, which are devoid of keratins, rendered the cells more resistant to killing by TNF. We also showed that overexpressed NH2 termini of K18 and K8/18 were associated with endogenous TRADD in SW13 cells, resulting in the inhibition of caspase-8 activation. These results indicate that K18 may sequester TRADD to attenuate interactions between TRADD and activated TNFR1 and moderate TNF-induced apoptosis in simple epithelial cells."xsd:string
http://purl.uniprot.org/citations/11684708http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200103078"xsd:string
http://purl.uniprot.org/citations/11684708http://purl.org/dc/terms/identifier"doi:10.1083/jcb.200103078"xsd:string
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/author"Nishizawa M."xsd:string
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/author"Nishizawa M."xsd:string
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/author"Kiyono T."xsd:string
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/author"Kiyono T."xsd:string
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/author"Takahashi T."xsd:string
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/author"Takahashi T."xsd:string
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/author"Inagaki M."xsd:string
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/author"Inagaki M."xsd:string
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/author"Izawa I."xsd:string
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/author"Izawa I."xsd:string
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/author"Momoi T."xsd:string
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/author"Momoi T."xsd:string
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/author"Fujita E."xsd:string
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/author"Fujita E."xsd:string
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/author"Inada H."xsd:string
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/author"Inada H."xsd:string
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/11684708http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string