Schrul, Bianca

[["dc.bibliographiccitation.journal","Matters"],["dc.contributor.author","Clancy, Anne"],["dc.contributor.author","Schrul, Bianca"],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2017-11-28T10:03:35Z"],["dc.date.available","2017-11-28T10:03:35Z"],["dc.date.issued","2016"],["dc.description.abstract","14-3-3 proteins are abundant modulators of cellular processes, in particular signal transduction. They function by binding to a broad spectrum of client proteins, thus affecting client protein localisation or function[1]Gardino 2011 [1]Morrison 2009 [2][2]. Animals and plants express 14-3-3 proteins encoded by several genes, which has made it difficult to study their unique rather than shared functions. The yeast Saccharomyces cerevisiae possesses only two highly homologous 14-3-3 genes, BMH1 and BMH2. Using this model system we now uncover novel aspects of functional specificity between the two yeast 14-3-3s. We show that bmh1 but not bmh2 cells display an altered morphology of the endomembrane system and specific trafficking defects under glucose starvation. This but not a second phenotype specific to the bmh1 strain, that is, the accumulation of glycogen, was rescued by overexpression of the nucleotide exchange factor Gea1, suggesting a role for Bmh1 in Gea1’s function or regulation."],["dc.identifier.doi","10.19185/matters.201609000004"],["dc.identifier.fs","626945"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/10613"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/61"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | Z03: Synthetische genetische Analyse, automatisierte Mikroskopie und Bildanalyse"],["dc.relation.issn","2297-8240"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.title","The guanine nucleotide exchange factor Gea1 rescues an isoform-specific 14-3-3 phenotype"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","unknown"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","405"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","420"],["dc.bibliographiccitation.volume","198"],["dc.contributor.author","Moreira, Karen E."],["dc.contributor.author","Schuck, Sebastian"],["dc.contributor.author","Schrul, Bianca"],["dc.contributor.author","Froehlich, Florian"],["dc.contributor.author","Moseley, James B."],["dc.contributor.author","Walther, Tobias C."],["dc.contributor.author","Walter, Peter"],["dc.date.accessioned","2018-11-07T09:07:18Z"],["dc.date.available","2018-11-07T09:07:18Z"],["dc.date.issued","2012"],["dc.description.abstract","Eisosomes are stable domains at the plasma membrane of the budding yeast Saccharomyces cerevisiae and have been proposed to function in endocytosis. Eisosomes are composed of two main cytoplasmic proteins, Pil1 and Lsp1, that form a scaffold around furrow-like plasma membrane invaginations. We show here that the poorly characterized eisosome protein Seg1/Ymr086w is important for eisosome biogenesis and architecture. Seg1 was required for efficient incorporation of Pil1 into eisosomes and the generation of normal plasma membrane furrows. Seg1 preceded Pil1 during eisosome formation and established a platform for the assembly of other eisosome components. This platform was further shaped and stabilized upon the arrival of Pil1 and Lsp1. Moreover, Seg1 abundance controlled the shape of eisosomes by determining their length. Similarly, the Schizosaccharomyces pombe Seg1-like protein Sle1 was necessary to generate the filamentous eisosomes present in fission yeast. The function of Seg1 in the stepwise biogenesis of eisosomes reveals striking architectural similarities between eisosomes in yeast and caveolae in mammals."],["dc.identifier.doi","10.1083/jcb.201202097"],["dc.identifier.isi","000307412200016"],["dc.identifier.pmid","22869600"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25762"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Rockefeller Univ Press"],["dc.relation.issn","1540-8140"],["dc.relation.issn","0021-9525"],["dc.title","Seg1 controls eisosome assembly and shape"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","jcs223016"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.volume","132"],["dc.contributor.author","Exner, Tarik"],["dc.contributor.author","Romero-Brey, Inés"],["dc.contributor.author","Yifrach, Eden"],["dc.contributor.author","Rivera-Monroy, Jhon"],["dc.contributor.author","Schrul, Bianca"],["dc.contributor.author","Zouboulis, Christos C."],["dc.contributor.author","Stremmel, Wolfgang"],["dc.contributor.author","Honsho, Masanori"],["dc.contributor.author","Bartenschlager, Ralf"],["dc.contributor.author","Zalckvar, Einat"],["dc.contributor.author","Poppelreuther, Margarete"],["dc.contributor.author","Füllekrug, Joachim"],["dc.date.accessioned","2020-12-10T18:41:53Z"],["dc.date.available","2020-12-10T18:41:53Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1242/jcs.223016"],["dc.identifier.eissn","1477-9137"],["dc.identifier.issn","0021-9533"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/77714"],["dc.language.iso","en"],["dc.notes.intern","DOI Import GROB-354"],["dc.title","An alternative membrane topology permits lipid droplet localization of peroxisomal fatty acyl-CoA reductase 1"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]