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http://purl.uniprot.org/citations/19520058http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19520058http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19520058http://www.w3.org/2000/01/rdf-schema#comment"Alix and TSG101, known to physically interact with each other, have Pro-rich regions that are bound by ALG-2 Ca2+-dependently. We investigated the role of ALG-2 in the Alix-TSG101 association by pulldown assays using Strep-tagged Alix and its various mutants. The ALG-2-binding site was required for the Ca2+-dependent pulldown of TSG101 using HEK293T cells, whereas the PSAP sequence, a binding motif for the UEV domain of TSG101, was dispensable. Alix-TSG101 association was not observed using ALG-2-knockdown cells but became detectable by addition of the purified recombinant ALG-2 protein in the assay mixtures. Exogenous expression of mGFP-fused ALG-2 also restored the pulldown capability of Strep-Alix, but an alternatively spliced shorter ALG-2 isoform and a dimerization-defective mutant were incompetent. Based on the X-ray crystal structure model showing the presence of one ligand-binding site in each molecule of an ALG-2 dimer, we propose that Ca2+-loaded ALG-2 bridges Alix and TSG101 as an adaptor protein."xsd:string
http://purl.uniprot.org/citations/19520058http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2009.06.015"xsd:string
http://purl.uniprot.org/citations/19520058http://purl.org/dc/terms/identifier"doi:10.1016/j.bbrc.2009.06.015"xsd:string
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/author"Suzuki H."xsd:string
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/author"Suzuki H."xsd:string
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/author"Yoshida H."xsd:string
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/author"Yoshida H."xsd:string
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/author"Maki M."xsd:string
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/author"Maki M."xsd:string
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/author"Shibata H."xsd:string
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/author"Shibata H."xsd:string
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/author"Kobayashi R."xsd:string
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/author"Kobayashi R."xsd:string
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/author"Okumura M."xsd:string
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/author"Okumura M."xsd:string
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/author"Ichioka F."xsd:string
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/author"Ichioka F."xsd:string
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/name"Biochem. Biophys. Res. Commun."xsd:string
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/pages"237-241"xsd:string
http://purl.uniprot.org/citations/19520058http://purl.uniprot.org/core/pages"237-241"xsd:string