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http://purl.uniprot.org/citations/33935042http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/33935042http://www.w3.org/2000/01/rdf-schema#comment"Phosphatidylserine (PS), a negatively charged phospholipid exclusively located in the inner leaflet of the plasma membrane, is involved in various cellular processes such as blood coagulation, myoblast fusion, mammalian fertilization, and clearance of apoptotic cells. Proteins that specifically interact with PS must be identified to comprehensively understand the cellular processes involving PS. However, only a limited number of proteins are known to associate with PS. To identify PS-associating proteins, we performed a pulldown assay using streptavidin-coated magnetic beads on which biotin-linked PS was immobilized. Using this approach, we identified Hsd17b4, a peroxisomal protein, as a PS-associating protein. Hsd17b4 strongly associated with PS, but not with phosphatidylcholine or sphingomyelin, and the Scp-2-like domain of Hsd17b4 was responsible for this association. The association was disrupted by PS in liposomes, but not by free PS or the components of PS. In addition, translocation of PS to the outer leaflet of the plasma membrane enriched Hsd17b4 in peroxisomes. Collectively, this study suggests an unexpected role of PS as a regulator of the subcellular localization of Hsd17b4."xsd:string
http://purl.uniprot.org/citations/33935042http://purl.org/dc/terms/identifier"doi:10.14348/molcells.2021.2217"xsd:string
http://purl.uniprot.org/citations/33935042http://purl.uniprot.org/core/author"Kim K."xsd:string
http://purl.uniprot.org/citations/33935042http://purl.uniprot.org/core/author"Lee G."xsd:string
http://purl.uniprot.org/citations/33935042http://purl.uniprot.org/core/author"Kim D."xsd:string
http://purl.uniprot.org/citations/33935042http://purl.uniprot.org/core/author"Lee J."xsd:string
http://purl.uniprot.org/citations/33935042http://purl.uniprot.org/core/author"Park D."xsd:string
http://purl.uniprot.org/citations/33935042http://purl.uniprot.org/core/author"Park H."xsd:string
http://purl.uniprot.org/citations/33935042http://purl.uniprot.org/core/author"Yang S."xsd:string
http://purl.uniprot.org/citations/33935042http://purl.uniprot.org/core/author"Moon H."xsd:string
http://purl.uniprot.org/citations/33935042http://purl.uniprot.org/core/author"Moon B."xsd:string
http://purl.uniprot.org/citations/33935042http://purl.uniprot.org/core/author"Park R."xsd:string
http://purl.uniprot.org/citations/33935042http://purl.uniprot.org/core/author"Lee S.A."xsd:string
http://purl.uniprot.org/citations/33935042http://purl.uniprot.org/core/author"Min C."xsd:string
http://purl.uniprot.org/citations/33935042http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/33935042http://purl.uniprot.org/core/name"Mol Cells"xsd:string
http://purl.uniprot.org/citations/33935042http://purl.uniprot.org/core/pages"214-222"xsd:string
http://purl.uniprot.org/citations/33935042http://purl.uniprot.org/core/title"The Peroxisomal Localization of Hsd17b4 Is Regulated by Its Interaction with Phosphatidylserine."xsd:string
http://purl.uniprot.org/citations/33935042http://purl.uniprot.org/core/volume"44"xsd:string
http://purl.uniprot.org/citations/33935042http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/33935042
http://purl.uniprot.org/citations/33935042http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/33935042
http://purl.uniprot.org/uniprot/#_A0A0S2Z460-mappedCitation-33935042http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33935042
http://purl.uniprot.org/uniprot/#_A0A0S2Z4Q6-mappedCitation-33935042http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33935042
http://purl.uniprot.org/uniprot/#_A0A0S2Z3Y5-mappedCitation-33935042http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/33935042