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.issue","11"],["dc.bibliographiccitation.journal","Journal of Cell Biology"],["dc.bibliographiccitation.volume","220"],["dc.contributor.author","Eisenberg-Bord, Michal"],["dc.contributor.author","Zung, Naama"],["dc.contributor.author","Collado, Javier"],["dc.contributor.author","Drwesh, Layla"],["dc.contributor.author","Fenech, Emma J."],["dc.contributor.author","Fadel, Amir"],["dc.contributor.author","Dezorella, Nili"],["dc.contributor.author","Bykov, Yury S."],["dc.contributor.author","Rapaport, Doron"],["dc.contributor.author","Fernández Busnadiego, Rubén"],["dc.contributor.author","Schuldiner, Maya"],["dc.date.accessioned","2021-12-01T09:21:03Z"],["dc.date.available","2021-12-01T09:21:03Z"],["dc.date.issued","2021"],["dc.description.abstract","Mitochondrial functions are tightly regulated by nuclear activity, requiring extensive communication between these organelles. One way by which organelles can communicate is through contact sites, areas of close apposition held together by tethering molecules. While many contacts have been characterized in yeast, the contact between the nucleus and mitochondria was not previously identified. Using fluorescence and electron microscopy in S. cerevisiae, we demonstrate specific areas of contact between the two organelles. Using a high-throughput screen, we uncover a role for the uncharacterized protein Ybr063c, which we have named Cnm1 (contact nucleus mitochondria 1), as a molecular tether on the nuclear membrane. We show that Cnm1 mediates contact by interacting with Tom70 on mitochondria. Moreover, Cnm1 abundance is regulated by phosphatidylcholine, enabling the coupling of phospholipid homeostasis with contact extent. The discovery of a molecular mechanism that allows mitochondrial crosstalk with the nucleus sets the ground for better understanding of mitochondrial functions in health and disease."],["dc.identifier.doi","10.1083/jcb.202104100"],["dc.identifier.pmid","34694322"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/94334"],["dc.identifier.url","https://mbexc.uni-goettingen.de/literature/publications/365"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/162"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-478"],["dc.relation","EXC 2067: Multiscale Bioimaging"],["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 Fernández-Busnadiego (Structural Cell Biology)"],["dc.relation.workinggroup","RG Schuldiner (Functional Genomics of Organelles)"],["dc.rights","CC BY 4.0"],["dc.title","Cnm1 mediates nucleus–mitochondria contact site formation in response to phospholipid levels"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.volume","219"],["dc.contributor.author","Wang, Yaxi"],["dc.contributor.author","Yuan, Peihua"],["dc.contributor.author","Grabon, Aby"],["dc.contributor.author","Tripathi, Ashutosh"],["dc.contributor.author","Lee, Dongju"],["dc.contributor.author","Rodriguez, Martin"],["dc.contributor.author","Lönnfors, Max"],["dc.contributor.author","Eisenberg-Bord, Michal"],["dc.contributor.author","Wang, Zehua"],["dc.contributor.author","Man Lam, Sin"],["dc.contributor.author","Schuldiner, Maya"],["dc.contributor.author","Bankaitis, Vytas A."],["dc.date.accessioned","2022-07-08T10:36:17Z"],["dc.date.available","2022-07-08T10:36:17Z"],["dc.date.issued","2020"],["dc.description.abstract","The yeast phosphatidylserine (PtdSer) decarboxylase Psd2 is proposed to engage in a membrane contact site (MCS) for PtdSer decarboxylation to phosphatidylethanolamine (PtdEtn). This proposed MCS harbors Psd2, the Sec14-like phosphatidylinositol transfer protein (PITP) Sfh4, the Stt4 phosphatidylinositol (PtdIns) 4-OH kinase, the Scs2 tether, and an uncharacterized protein. We report that, of these components, only Sfh4 and Stt4 regulate Psd2 activity in vivo. They do so via distinct mechanisms. Sfh4 operates via a mechanism for which its PtdIns-transfer activity is dispensable but requires an Sfh4-Psd2 physical interaction. The other requires Stt4-mediated production of PtdIns-4-phosphate (PtdIns4P), where Stt4 (along with the Sac1 PtdIns4P phosphatase and endoplasmic reticulum-plasma membrane tethers) indirectly modulate Psd2 activity via a PtdIns4P homeostatic mechanism that influences PtdSer accessibility to Psd2. These results identify an example in which the biological function of a Sec14-like PITP is cleanly uncoupled from its canonical in vitro PtdIns-transfer activity and challenge popular functional assumptions regarding lipid-transfer protein involvements in MCS function."],["dc.identifier.doi","10.1083/jcb.201907128"],["dc.identifier.pmid","32303746"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/112413"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/111"],["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 Schuldiner (Functional Genomics of Organelles)"],["dc.rights","CC BY-NC-SA 4.0"],["dc.title","Noncanonical regulation of phosphatidylserine metabolism by a Sec14-like protein and a lipid kinase"],["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"]]