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http://purl.uniprot.org/citations/10791968http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10791968http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10791968http://www.w3.org/2000/01/rdf-schema#comment"Epsin (Eps15 interactor) is a cytosolic protein involved in clathrin-mediated endocytosis via its direct interactions with clathrin, the clathrin adaptor AP-2, and Eps15. The NH(2)-terminal portion of epsin contains a phylogenetically conserved module of unknown function, known as the ENTH domain (epsin NH(2)-terminal homology domain). We have now solved the crystal structure of rat epsin 1 ENTH domain to 1.8 A resolution. This domain is structurally similar to armadillo and Heat repeats of beta-catenin and karyopherin-beta, respectively. We have also identified and characterized the interaction of epsin 1, via the ENTH domain, with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF). Leptomycin B, an antifungal antibiotic, which inhibits the Crm1-dependent nuclear export pathway, induces an accumulation of epsin 1 in the nucleus. These findings suggest that epsin 1 may function in a signaling pathway connecting the endocytic machinery to the regulation of nuclear function."xsd:string
http://purl.uniprot.org/citations/10791968http://purl.org/dc/terms/identifier"doi:10.1083/jcb.149.3.537"xsd:string
http://purl.uniprot.org/citations/10791968http://purl.org/dc/terms/identifier"doi:10.1083/jcb.149.3.537"xsd:string
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/author"Chen H."xsd:string
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/author"Chen H."xsd:string
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/author"Brunger A.T."xsd:string
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/author"Brunger A.T."xsd:string
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/author"Di Fiore P.P."xsd:string
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/author"Di Fiore P.P."xsd:string
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/author"De Camilli P."xsd:string
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/author"De Camilli P."xsd:string
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/author"Hyman J."xsd:string
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/author"Hyman J."xsd:string
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/name"J. Cell Biol."xsd:string
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/pages"537-546"xsd:string
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/pages"537-546"xsd:string
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/title"Epsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo and Heat repeats, interacts with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF)."xsd:string
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/title"Epsin 1 undergoes nucleocytosolic shuttling and its eps15 interactor NH(2)-terminal homology (ENTH) domain, structurally similar to Armadillo and Heat repeats, interacts with the transcription factor promyelocytic leukemia Zn(2)+ finger protein (PLZF)."xsd:string
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/volume"149"xsd:string
http://purl.uniprot.org/citations/10791968http://purl.uniprot.org/core/volume"149"xsd:string