Bohnert, Maria

[["dc.bibliographiccitation.firstpage","269"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","282"],["dc.bibliographiccitation.volume","217"],["dc.contributor.author","Eisenberg-Bord, Michal"],["dc.contributor.author","Mari, Muriel"],["dc.contributor.author","Weill, Uri"],["dc.contributor.author","Rosenfeld-Gur, Eden"],["dc.contributor.author","Moldavski, Ofer"],["dc.contributor.author","Castro, Inês G."],["dc.contributor.author","Soni, Krishnakant G."],["dc.contributor.author","Harpaz, Nofar"],["dc.contributor.author","Levine, Tim P"],["dc.contributor.author","Futerman, Anthony H."],["dc.contributor.author","Reggiori, Fulvio"],["dc.contributor.author","Bankaitis, Vytas A."],["dc.contributor.author","Schuldiner, Maya"],["dc.contributor.author","Bohnert, Maria"],["dc.date.accessioned","2022-07-04T12:38:21Z"],["dc.date.available","2022-07-04T12:38:21Z"],["dc.date.issued","2018"],["dc.description.abstract","Functional heterogeneity within the lipid droplet (LD) pool of a single cell has been observed, yet the underlying mechanisms remain enigmatic. Here, we report on identification of a specialized LD subpopulation characterized by a unique proteome and a defined geographical location at the nucleus-vacuole junction contact site. In search for factors determining identity of these LDs, we screened ∼6,000 yeast mutants for loss of targeting of the subpopulation marker Pdr16 and identified Ldo45 (LD organization protein of 45 kD) as a crucial targeting determinant. Ldo45 is the product of a splicing event connecting two adjacent genes (YMR147W and YMR148W/OSW5/LDO16). We show that Ldo proteins cooperate with the LD biogenesis component seipin and establish LD identity by defining positioning and surface-protein composition. Our studies suggest a mechanism to establish functional differentiation of organelles, opening the door to better understanding of metabolic decisions in cells."],["dc.identifier.doi","10.1083/jcb.201704122"],["dc.identifier.pmid","29187527"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112374"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/17"],["dc.language.iso","en"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P11: Zuordnung zellulärer Kontaktstellen und deren Zusammenspiel"],["dc.relation.eissn","1540-8140"],["dc.relation.issn","0021-9525"],["dc.relation.workinggroup","RG Bohnert (Lipid Droplet Kommunikation)"],["dc.relation.workinggroup","RG Schuldiner (Functional Genomics of Organelles)"],["dc.rights","CC BY 4.0"],["dc.title","Identification of seipin-linked factors that act as determinants of a lipid droplet subpopulation"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","268"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Cells"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Castro, Inês G."],["dc.contributor.author","Eisenberg-Bord, Michal"],["dc.contributor.author","Persiani, Elisa"],["dc.contributor.author","Rochford, Justin J."],["dc.contributor.author","Schuldiner, Maya"],["dc.contributor.author","Bohnert, Maria"],["dc.date.accessioned","2022-07-04T14:24:51Z"],["dc.date.available","2022-07-04T14:24:51Z"],["dc.date.issued","2019"],["dc.description.abstract","Seipin (BSCL2/SPG17) is a key factor in lipid droplet (LD) biology, and its dysfunction results in severe pathologies, including the fat storage disease Berardinelli-Seip congenital lipodystrophy type 2, as well as several neurological seipinopathies. Despite its importance for human health, the molecular role of seipin is still enigmatic. Seipin is evolutionarily conserved from yeast to humans. In yeast, seipin was recently found to cooperate with the lipid droplet organization (LDO) proteins, Ldo16 and Ldo45, two structurally-related proteins involved in LD function and identity that display remote homology to the human protein promethin/TMEM159. In this study, we show that promethin is indeed an LD-associated protein that forms a complex with seipin, and its localization to the LD surface can be modulated by seipin expression levels. We thus identify promethin as a novel seipin partner protein."],["dc.identifier.doi","10.3390/cells8030268"],["dc.identifier.pmid","30901948"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112383"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/62"],["dc.language.iso","en"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P11: Zuordnung zellulärer Kontaktstellen und deren Zusammenspiel"],["dc.relation.issn","2073-4409"],["dc.relation.workinggroup","RG Bohnert (Lipid Droplet Kommunikation)"],["dc.relation.workinggroup","RG Schuldiner (Functional Genomics of Organelles)"],["dc.rights","CC BY 4.0"],["dc.title","Promethin Is a Conserved Seipin Partner Protein"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]