{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1360021396524593792.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1242/jcs.205435"}},{"identifier":{"@type":"URI","@value":"https://syndication.highwire.org/content/doi/10.1242/jcs.205435"}},{"identifier":{"@type":"URI","@value":"https://journals.biologists.com/jcs/article-pdf/130/22/3891/3500387/jcs205435.pdf"}},{"identifier":{"@type":"URI","@value":"http://journals.biologists.com/jcs/article-pdf/doi/10.1242/jcs.205435/2058455/jcs_205435v1.pdf"}}],"dc:title":[{"@value":"Lipid-dependent regulation of exocytosis in <i>S. cerevisiae</i> by OSBP homolog (Osh) 4"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:title>ABSTRACT</jats:title>\n               <jats:p>Polarized exocytosis is an essential process in many organisms and cell types for correct cell division or functional specialization. Previous studies established that homologs of the oxysterol-binding protein (OSBP) in S. cerevisiae, which comprise the Osh protein family, are necessary for efficient polarized exocytosis by supporting a late post-Golgi step. We define this step as the docking of a specific sub-population of exocytic vesicles with the plasma membrane. In the absence of other Osh proteins, yeast Osh4p can support this process in a manner dependent upon two lipid ligands, PI4P and sterol. Osh6p, which binds PI4P and phosphatidylserine, is also sufficient to support polarized exocytosis, again in a lipid-dependent manner. These data suggest that Osh-mediated exocytosis depends upon lipid binding and exchange without a strict requirement for sterol. We propose a two-step mechanism for Osh protein-mediated regulation of polarized exocytosis by using Osh4p as a model. We describe a specific in vivo role for lipid binding by an OSBP-related protein (ORP) in the process of polarized exocytosis, guiding our understanding of where and how OSBP and ORPs may function in more complex organisms.</jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1380021396524593793","@type":"Researcher","foaf:name":[{"@value":"Richard J. Smindak"}],"jpcoar:affiliationName":[{"@value":"University of Virginia 1 Department of Biology , , Charlottesville, VA 22904, USA"}]},{"@id":"https://cir.nii.ac.jp/crid/1380021396524593797","@type":"Researcher","foaf:name":[{"@value":"Lindsay A. Heckle"}],"jpcoar:affiliationName":[{"@value":"University of Virginia 1 Department of Biology , , Charlottesville, VA 22904, USA"}]},{"@id":"https://cir.nii.ac.jp/crid/1380021396524593796","@type":"Researcher","foaf:name":[{"@value":"Supraja S. Chittari"}],"jpcoar:affiliationName":[{"@value":"University of Virginia 1 Department of Biology , , Charlottesville, VA 22904, USA"}]},{"@id":"https://cir.nii.ac.jp/crid/1380021396524593792","@type":"Researcher","foaf:name":[{"@value":"Marissa A. Hand"}],"jpcoar:affiliationName":[{"@value":"University of Virginia 1 Department of Biology , , Charlottesville, VA 22904, USA"}]},{"@id":"https://cir.nii.ac.jp/crid/1380021396524593798","@type":"Researcher","foaf:name":[{"@value":"Dylan M. Hyatt"}],"jpcoar:affiliationName":[{"@value":"University of Virginia 1 Department of Biology , , Charlottesville, VA 22904, USA"}]},{"@id":"https://cir.nii.ac.jp/crid/1380021396524593795","@type":"Researcher","foaf:name":[{"@value":"Grace E. Mantus"}],"jpcoar:affiliationName":[{"@value":"University of Virginia 1 Department of Biology , , Charlottesville, VA 22904, USA"}]},{"@id":"https://cir.nii.ac.jp/crid/1380021396524593794","@type":"Researcher","foaf:name":[{"@value":"William A. Sanfelippo"}],"jpcoar:affiliationName":[{"@value":"University of Virginia 1 Department of Biology , , Charlottesville, VA 22904, USA"}]},{"@id":"https://cir.nii.ac.jp/crid/1380021396524593799","@type":"Researcher","foaf:name":[{"@value":"Keith G. Kozminski"}],"jpcoar:affiliationName":[{"@value":"University of Virginia 1 Department of Biology , , Charlottesville, VA 22904, USA"},{"@value":"University of Virginia 2 Department of Cell Biology , , Charlottesville, VA 22908, USA"}]}],"publication":{"publicationIdentifier":[{"@type":"EISSN","@value":"14779137"},{"@type":"PISSN","@value":"00219533"}],"prism:publicationName":[{"@value":"Journal of Cell Science"}],"dc:publisher":[{"@value":"The Company of Biologists"}],"prism:publicationDate":"2017-11-15","prism:volume":"130","prism:number":"22","prism:startingPage":"3891","prism:endingPage":"3906"},"reviewed":"false","dc:rights":["http://www.biologists.com/user-licence-1-1/"],"url":[{"@id":"https://syndication.highwire.org/content/doi/10.1242/jcs.205435"},{"@id":"https://journals.biologists.com/jcs/article-pdf/130/22/3891/3500387/jcs205435.pdf"},{"@id":"http://journals.biologists.com/jcs/article-pdf/doi/10.1242/jcs.205435/2058455/jcs_205435v1.pdf"}],"createdAt":"2017-10-10","modifiedAt":"2024-06-13","relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1360584341809949696","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Coordinated regulation of phosphatidylinositol 4-phosphate and phosphatidylserine levels by Osh4p and Osh5p is an essential regulatory mechanism in autophagy"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1242/jcs.205435"},{"@type":"CROSSREF","@value":"10.1016/j.bbamem.2024.184308_references_DOI_aRLZPghCv0gAZvH3dSXXwuEfnHP"}]}