Schwappach-Pignataro, Blanche

[["dc.bibliographiccitation.firstpage","1055"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","FEMS Yeast Research"],["dc.bibliographiccitation.lastpage","1067"],["dc.bibliographiccitation.volume","14"],["dc.contributor.author","Elbaz-Alon, Yael"],["dc.contributor.author","Morgan, Bruce"],["dc.contributor.author","Clancy, Anne"],["dc.contributor.author","Amoako, Theresa N. E."],["dc.contributor.author","Zalckvar, Einat"],["dc.contributor.author","Dick, Tobias P."],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Schuldiner, Maya"],["dc.date.accessioned","2017-09-07T11:45:25Z"],["dc.date.available","2017-09-07T11:45:25Z"],["dc.date.issued","2014"],["dc.description.abstract","Glutathione, the most abundant small-molecule thiol in eukaryotic cells, is synthesized de novo solely in the cytosol and must subsequently be transported to other cellular compartments. The mechanisms of glutathione transport into and out of organelles remain largely unclear. We show that budding yeast Opt2, a close homolog of the plasma membrane glutathione transporter Opt1, localizes to peroxisomes. We demonstrate that deletion of OPT2 leads to major defects in maintaining peroxisomal, mitochondrial, and cytosolic glutathione redox homeostasis. Furthermore, opt2 strains display synthetic lethality with deletions of genes central to iron homeostasis that require mitochondrial glutathione redox homeostasis. Our results shed new light on the importance of peroxisomes in cellular glutathione homeostasis."],["dc.identifier.doi","10.1111/1567-1364.12196"],["dc.identifier.gro","3142025"],["dc.identifier.isi","000344918500007"],["dc.identifier.pmid","25130273"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/3712"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Wiley-blackwell"],["dc.relation.eissn","1567-1364"],["dc.relation.issn","1567-1356"],["dc.title","The yeast oligopeptide transporter Opt2 is localized to peroxisomes and affects glutathione redox homeostasis"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","134"],["dc.bibliographiccitation.issue","7631"],["dc.bibliographiccitation.journal","Nature"],["dc.bibliographiccitation.lastpage","138"],["dc.bibliographiccitation.volume","540"],["dc.contributor.author","Aviram, Naama"],["dc.contributor.author","Ast, Tslil"],["dc.contributor.author","Costa, Elizabeth A."],["dc.contributor.author","Arakel, Eric C."],["dc.contributor.author","Chuartzman, Silvia G."],["dc.contributor.author","Jan, Calvin H."],["dc.contributor.author","Haßdenteufel, Sarah"],["dc.contributor.author","Dudek, Johanna"],["dc.contributor.author","Jung, Martin"],["dc.contributor.author","Schorr, Stefan"],["dc.contributor.author","Zimmermann, Richard"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Weissman, Jonathan S."],["dc.contributor.author","Schuldiner, Maya"],["dc.date.accessioned","2018-04-23T11:49:05Z"],["dc.date.available","2018-04-23T11:49:05Z"],["dc.date.issued","2016"],["dc.description.abstract","In eukaryotes, up to one-third of cellular proteins are targeted to the endoplasmic reticulum, where they undergo folding, processing, sorting and trafficking to subsequent endomembrane compartments. Targeting to the endoplasmic reticulum has been shown to occur co-translationally by the signal recognition particle (SRP) pathway or post-translationally by the mammalian transmembrane recognition complex of 40 kDa (TRC40) and homologous yeast guided entry of tail-anchored proteins (GET) pathways. Despite the range of proteins that can be catered for by these two pathways, many proteins are still known to be independent of both SRP and GET, so there seems to be a critical need for an additional dedicated pathway for endoplasmic reticulum relay. We set out to uncover additional targeting proteins using unbiased high-content screening approaches. To this end, we performed a systematic visual screen using the yeast Saccharomyces cerevisiae and uncovered three uncharacterized proteins whose loss affected targeting. We suggest that these proteins work together and demonstrate that they function in parallel with SRP and GET to target a broad range of substrates to the endoplasmic reticulum. The three proteins, which we name Snd1, Snd2 and Snd3 (for SRP-independent targeting), can synthetically compensate for the loss of both the SRP and GET pathways, and act as a backup targeting system. This explains why it has previously been difficult to demonstrate complete loss of targeting for some substrates. Our discovery thus puts in place an essential piece of the endoplasmic reticulum targeting puzzle, highlighting how the targeting apparatus of the eukaryotic cell is robust, interlinked and flexible."],["dc.identifier.doi","10.1038/nature20169"],["dc.identifier.gro","3142487"],["dc.identifier.pmid","27905431"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13639"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/3"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation.issn","0028-0836"],["dc.relation.workinggroup","RG Schuldiner (Functional Genomics of Organelles)"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.title","The SND proteins constitute an alternative targeting route to the endoplasmic reticulum"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2389"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],["dc.bibliographiccitation.lastpage","2391"],["dc.bibliographiccitation.volume","1833"],["dc.contributor.author","Schuldiner, Maya"],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2017-09-07T11:47:05Z"],["dc.date.available","2017-09-07T11:47:05Z"],["dc.date.issued","2013"],["dc.identifier.doi","10.1016/j.bbamcr.2013.03.005"],["dc.identifier.gro","3142265"],["dc.identifier.isi","000323400000001"],["dc.identifier.pmid","23500901"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6365"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0167-4889"],["dc.title","From rags to riches - The history of the endoplasmic reticulum Preface"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","letter_note"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","jcs211110"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.volume","131"],["dc.contributor.author","Vitali, Daniela G."],["dc.contributor.author","Sinzel, Monika"],["dc.contributor.author","Bulthuis, Elianne P."],["dc.contributor.author","Kolb, Antonia"],["dc.contributor.author","Zabel, Susanne"],["dc.contributor.author","Mehlhorn, Dietmar G."],["dc.contributor.author","Figueiredo Costa, Bruna"],["dc.contributor.author","Farkas, Ákos"],["dc.contributor.author","Clancy, Anne"],["dc.contributor.author","Schuldiner, Maya"],["dc.contributor.author","Grefen, Christopher"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Borgese, Nica"],["dc.contributor.author","Rapaport, Doron"],["dc.date.accessioned","2020-12-10T18:41:52Z"],["dc.date.available","2020-12-10T18:41:52Z"],["dc.date.issued","2018"],["dc.identifier.doi","10.1242/jcs.211110"],["dc.identifier.pmid","29661846"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77708"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/60"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P04: Der GET-Rezeptor als ein Eingangstor zum ER und sein Zusammenspiel mit GET bodies"],["dc.relation.workinggroup","RG Schuldiner (Functional Genomics of Organelles)"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.title","The GET pathway can increase the risk of mitochondrial outer membrane proteins to be mistargeted to the ER"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1693"],["dc.bibliographiccitation.issue","5922"],["dc.bibliographiccitation.journal","Science"],["dc.bibliographiccitation.lastpage","1697"],["dc.bibliographiccitation.volume","323"],["dc.contributor.author","Jonikas, Martin C."],["dc.contributor.author","Collins, Sean R."],["dc.contributor.author","Denic, Vladimir"],["dc.contributor.author","Oh, Eugene"],["dc.contributor.author","Quan, Erin M."],["dc.contributor.author","Schmid, Volker"],["dc.contributor.author","Weibezahn, Jimena"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Walter, Peter"],["dc.contributor.author","Weissman, Jonathan S."],["dc.contributor.author","Schuldiner, Maya"],["dc.date.accessioned","2017-09-07T11:47:32Z"],["dc.date.available","2017-09-07T11:47:32Z"],["dc.date.issued","2009"],["dc.description.abstract","Protein folding in the endoplasmic reticulum is a complex process whose malfunction is implicated in disease and aging. By using the cell's endogenous sensor (the unfolded protein response), we identified several hundred yeast genes with roles in endoplasmic reticulum folding and systematically characterized their functional interdependencies by measuring unfolded protein response levels in double mutants. This strategy revealed multiple conserved factors critical for endoplasmic reticulum folding, including an intimate dependence on the later secretory pathway, a previously uncharacterized six-protein transmembrane complex, and a co-chaperone complex that delivers tail-anchored proteins to their membrane insertion machinery. The use of a quantitative reporter in a comprehensive screen followed by systematic analysis of genetic dependencies should be broadly applicable to functional dissection of complex cellular processes from yeast to human."],["dc.identifier.doi","10.1126/science.1167983"],["dc.identifier.gro","3143135"],["dc.identifier.isi","000264559800030"],["dc.identifier.pmid","19325107"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/616"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0036-8075"],["dc.title","Comprehensive Characterization of Genes Required for Protein Folding in the Endoplasmic Reticulum"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Aviram, N."],["dc.contributor.author","Ast, T."],["dc.contributor.author","Hassdenteufel, S."],["dc.contributor.author","Costa, E. A."],["dc.contributor.author","Arakel, E. C."],["dc.contributor.author","Schorr, Stefan"],["dc.contributor.author","Chuartzman, Silvia G."],["dc.contributor.author","Jan, C. H."],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Zimmermann, R."],["dc.contributor.author","Weissman, J. S."],["dc.contributor.author","Schuldiner, Maya"],["dc.date.accessioned","2018-11-07T10:04:15Z"],["dc.date.available","2018-11-07T10:04:15Z"],["dc.date.issued","2015"],["dc.identifier.isi","000209928401009"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/38656"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Cell Biology"],["dc.publisher.place","Bethesda"],["dc.title","The SND proteins target SRP-independent substrates to the endoplasmic reticulum."],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]