Arakel, Eric Clement

[["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","672"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","Traffic"],["dc.bibliographiccitation.lastpage","682"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Geva, Yosef"],["dc.contributor.author","Crissman, Jonathan"],["dc.contributor.author","Arakel, Eric C."],["dc.contributor.author","Gómez-Navarro, Natalia"],["dc.contributor.author","Chuartzman, Silvia G."],["dc.contributor.author","Stahmer, Kyle R."],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Miller, Elizabeth A."],["dc.contributor.author","Schuldiner, Maya"],["dc.date.accessioned","2018-04-23T11:49:04Z"],["dc.date.available","2018-04-23T11:49:04Z"],["dc.date.issued","2017"],["dc.description.abstract","The endoplasmic reticulum (ER) is the entry site of proteins into the endomembrane system. Proteins exit the ER via coat protein II (COPII) vesicles in a selective manner, mediated either by direct interaction with the COPII coat or aided by cargo receptors. Despite the fundamental role of such receptors in protein sorting, only a few have been identified. To further define the machinery that packages secretory cargo and targets proteins from the ER to Golgi membranes, we used multiple systematic approaches, which revealed 2 uncharacterized proteins that mediate the trafficking and maturation of Pma1, the essential yeast plasma membrane proton ATPase. Ydl121c (Exp1) is an ER protein that binds Pma1, is packaged into COPII vesicles, and whose deletion causes ER retention of Pma1. Ykl077w (Psg1) physically interacts with Exp1 and can be found in the Golgi and coat protein I (COPI) vesicles but does not directly bind Pma1. Loss of Psg1 causes enhanced degradation of Pma1 in the vacuole. Our findings suggest that Exp1 is a Pma1 cargo receptor and that Psg1 aids Pma1 maturation in the Golgi or affects its retrieval. More generally our work shows the utility of high content screens in the identification of novel trafficking components."],["dc.identifier.doi","10.1111/tra.12503"],["dc.identifier.gro","3142485"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13637"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/11"],["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","SFB 1190 | P11: Zuordnung zellulärer Kontaktstellen und deren Zusammenspiel"],["dc.relation.issn","1398-9219"],["dc.relation.workinggroup","RG Schuldiner (Functional Genomics of Organelles)"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.rights","CC BY 4.0"],["dc.title","Two novel effectors of trafficking and maturation of the yeast plasma membrane H+-ATPase"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dc.type.subtype","overview_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","370"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Traffic"],["dc.bibliographiccitation.lastpage","379"],["dc.bibliographiccitation.volume","19"],["dc.contributor.author","Weill, Uri"],["dc.contributor.author","Arakel, Eric C."],["dc.contributor.author","Goldmann, Omer"],["dc.contributor.author","Golan, Matan"],["dc.contributor.author","Chuartzman, Silvia"],["dc.contributor.author","Munro, Sean"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Schuldiner, Maya"],["dc.date.accessioned","2020-12-10T18:36:31Z"],["dc.date.available","2020-12-10T18:36:31Z"],["dc.date.issued","2018"],["dc.description.abstract","A third of yeast genes encode for proteins that function in the endomembrane system. However, the precise localization for many of these proteins is still uncertain. Here, we visualized a collection of ~500 N-terminally, green fluorescent protein (GFP), tagged proteins of the yeast Saccharomyces cerevisiae. By co-localizing them with 7 known markers of endomembrane compartments we determined the localization for over 200 of them. Using this approach, we create a systematic database of the various secretory compartments and identify several new residents. Focusing in, we now suggest that Lam5 resides in contact sites between the endoplasmic reticulum and the late Golgi. Additionally, analysis of interactions between the COPI coat and co-localizing proteins from our screen identifies a subset of proteins that are COPI-cargo. In summary, our approach defines the protein roster within each compartment enabling characterization of the physical and functional organization of the endomembrane system and its components."],["dc.identifier.doi","10.1111/tra.12560"],["dc.identifier.pmid","29527758"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/76654"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/24"],["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","SFB 1190 | P11: Zuordnung zellulärer Kontaktstellen und deren Zusammenspiel"],["dc.relation","SFB 1190 | Z03: Synthetische genetische Analyse, automatisierte Mikroskopie und Bildanalyse"],["dc.relation.issn","1398-9219"],["dc.relation.workinggroup","RG Schuldiner (Functional Genomics of Organelles)"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.rights","CC BY 4.0"],["dc.title","Toolbox: Creating a systematic database of secretory pathway proteins uncovers new cargo for COPI"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["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"]]