Schuldiner, Maya

[["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","483"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Nature Reviews. Molecular Cell Biology"],["dc.bibliographiccitation.lastpage","484"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Bohnert, Maria"],["dc.contributor.author","Schuldiner, Maya"],["dc.date.accessioned","2022-07-11T15:20:59Z"],["dc.date.available","2022-07-11T15:20:59Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1038/s41580-018-0022-1"],["dc.identifier.pmid","29765158"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112466"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/88"],["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","1471-0080"],["dc.relation.issn","1471-0072"],["dc.relation.workinggroup","RG Schuldiner (Functional Genomics of Organelles)"],["dc.relation.workinggroup","RG Bohnert (Lipid Droplet Kommunikation)"],["dc.title","Stepping outside the comfort zone of membrane contact site research"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","overview_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","395"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Developmental Cell"],["dc.bibliographiccitation.lastpage","409"],["dc.bibliographiccitation.volume","39"],["dc.contributor.author","Eisenberg-Bord, Michal"],["dc.contributor.author","Shai, Nadav"],["dc.contributor.author","Schuldiner, Maya"],["dc.contributor.author","Bohnert, Maria"],["dc.date.accessioned","2022-07-11T15:02:22Z"],["dc.date.available","2022-07-11T15:02:22Z"],["dc.date.issued","2016"],["dc.description.abstract","Membrane contact sites enable interorganelle communication by positioning organelles in close proximity using molecular \"tethers.\" With a growing understanding of the importance of contact sites, the hunt for new contact sites and their tethers is in full swing. Determining just what is a tether has proven challenging. Here, we aim to delineate guidelines that define the prerequisites for categorizing a protein as a tether. Setting this gold standard now, while groups from different disciplines are beginning to explore membrane contact sites, will enable efficient cooperation in the growing field and help to realize a great collaborative opportunity to boost its development."],["dc.identifier.doi","10.1016/j.devcel.2016.10.022"],["dc.identifier.pmid","27875684"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112461"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/4"],["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","1878-1551"],["dc.relation.issn","1534-5807"],["dc.relation.workinggroup","RG Bohnert (Lipid Droplet Kommunikation)"],["dc.relation.workinggroup","RG Schuldiner (Functional Genomics of Organelles)"],["dc.title","A Tether Is a Tether Is a Tether: Tethering at Membrane Contact Sites"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.subtype","overview_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1188"],["dc.bibliographiccitation.issue","10, Pt. B"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta. Molecular and Cell Biology of Lipids"],["dc.bibliographiccitation.lastpage","1196"],["dc.bibliographiccitation.volume","1862"],["dc.contributor.author","Schuldiner, Maya"],["dc.contributor.author","Bohnert, Maria"],["dc.date.accessioned","2022-07-11T15:51:36Z"],["dc.date.available","2022-07-11T15:51:36Z"],["dc.date.issued","2017-10"],["dc.description.abstract","Lipid droplets (LDs) store lipids and hence serve as energy reservoir and as a source for building-blocks for the organelle membrane systems. LD biology therefore depends on tight communication with other organelles. The unique architecture of LDs, consisting of a neutral lipid core shielded by a phospholipid-monolayer, is however an obstacle to bulk-exchange of bilayer-bounded vesicles with other organelles. In recent years, it is emerging that contact sites, places where two organelles are positioned in close proximity allowing vesicle-independent communication, are an important way to integrate LDs into the organellar landscape. However, few LD contact sites have been studied in depth and our understanding of their structure, extent and function is only starting to emerge. Here, we highlight recent findings on the functions of LD contact sites and on the proteins involved in their formation and hypothesize about the unique characteristics of the contact sites formed by these intriguing organelles. This article is part of a Special Issue entitled: Recent Advances in Lipid Droplet Biology edited by Rosalind Coleman and Matthijs Hesselink."],["dc.identifier.doi","10.1016/j.bbalip.2017.06.005"],["dc.identifier.pmid","28627434"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112473"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/27"],["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","1388-1981"],["dc.relation.workinggroup","RG Bohnert (Lipid Droplet Kommunikation)"],["dc.relation.workinggroup","RG Schuldiner (Functional Genomics of Organelles)"],["dc.rights","CC BY-NC-ND 4.0"],["dc.title","A different kind of love - lipid droplet contact sites"],["dc.type","journal_article"],["dc.type.internalPublication","no"],["dc.type.subtype","overview_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2836"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","2852"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Morgenstern, Marcel"],["dc.contributor.author","Stiller, Sebastian B."],["dc.contributor.author","Lübbert, Philipp"],["dc.contributor.author","Peikert, Christian D."],["dc.contributor.author","Dannenmaier, Stefan"],["dc.contributor.author","Drepper, Friedel"],["dc.contributor.author","Weill, Uri"],["dc.contributor.author","Höß, Philipp"],["dc.contributor.author","Feuerstein, Reinhild"],["dc.contributor.author","Gebert, Michael"],["dc.contributor.author","Bohnert, Maria"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Schuldiner, Maya"],["dc.contributor.author","Schütze, Conny"],["dc.contributor.author","Oeljeklaus, Silke"],["dc.contributor.author","Pfanner, Nikolaus"],["dc.contributor.author","Wiedemann, Nils"],["dc.contributor.author","Warscheid, Bettina"],["dc.date.accessioned","2022-07-06T07:42:11Z"],["dc.date.available","2022-07-06T07:42:11Z"],["dc.date.issued","2017"],["dc.description.abstract","Mitochondria perform central functions in cellular bioenergetics, metabolism, and signaling, and their dysfunction has been linked to numerous diseases. The available studies cover only part of the mitochondrial proteome, and a separation of core mitochondrial proteins from associated fractions has not been achieved. We developed an integrative experimental approach to define the proteome of yeast mitochondria. We classified > 3,300 proteins of mitochondria and mitochondria-associated fractions and defined 901 high-confidence mitochondrial proteins, expanding the set of mitochondrial proteins by 82. Our analysis includes protein abundance under fermentable and nonfermentable growth, submitochondrial localization, single-protein experiments, and subcellular classification of mitochondria-associated fractions. We identified mitochondrial interactors of respiratory chain supercomplexes, ATP synthase, AAA proteases, the mitochondrial contact site and cristae organizing system (MICOS), and the coenzyme Q biosynthesis cluster, as well as mitochondrial proteins with dual cellular localization. The integrative proteome provides a high-confidence source for the characterization of physiological and pathophysiological functions of mitochondria and their integration into the cellular environment."],["dc.identifier.doi","10.1016/j.celrep.2017.06.014"],["dc.identifier.pmid","28658629"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112399"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/92"],["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","2211-1247"],["dc.relation.workinggroup","RG Bohnert (Lipid Droplet Kommunikation)"],["dc.relation.workinggroup","RG Schuldiner (Functional Genomics of Organelles)"],["dc.rights","CC BY-NC-ND 4.0"],["dc.title","Definition of a High-Confidence Mitochondrial Proteome at Quantitative Scale"],["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"]]