Now showing 1 - 2 of 2
  • 2016Journal Article Research Paper
    [["dc.bibliographiccitation.artnumber","39464"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Scientific Reports"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Rivera-Monroy, Jhon"],["dc.contributor.author","Musiol, Lena"],["dc.contributor.author","Unthan-Fechner, Kirsten"],["dc.contributor.author","Farkas, Ákos"],["dc.contributor.author","Clancy, Anne"],["dc.contributor.author","Coy-Vergara, Javier"],["dc.contributor.author","Weill, Uri"],["dc.contributor.author","Gockel, Sarah"],["dc.contributor.author","Lin, Shuh-Yow"],["dc.contributor.author","Corey, David P."],["dc.contributor.author","Kohl, Tobias"],["dc.contributor.author","Ströbel, Philipp"],["dc.contributor.author","Schuldiner, Maya"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","Vilardi, Fabio"],["dc.date.accessioned","2018-04-23T11:49:05Z"],["dc.date.available","2018-04-23T11:49:05Z"],["dc.date.issued","2016"],["dc.description.abstract","Tail-anchored (TA) proteins are post-translationally inserted into membranes. The TRC40 pathway targets TA proteins to the endoplasmic reticulum via a receptor comprised of WRB and CAML. TRC40 pathway clients have been identified using in vitro assays, however, the relevance of the TRC40 pathway in vivo remains unknown. We followed the fate of TA proteins in two tissue-specific WRB knockout mouse models and found that their dependence on the TRC40 pathway in vitro did not predict their reaction to receptor depletion in vivo. The SNARE syntaxin 5 (Stx5) was extremely sensitive to disruption of the TRC40 pathway. Screening yeast TA proteins with mammalian homologues, we show that the particular sensitivity of Stx5 is conserved, possibly due to aggregation propensity of its cytoplasmic domain. We establish that Stx5 is an autophagy target that is inefficiently membrane-targeted by alternative pathways. Our results highlight an intimate relationship between the TRC40 pathway and cellular proteostasis."],["dc.identifier.doi","10.1038/srep39464"],["dc.identifier.gro","3142486"],["dc.identifier.pmid","28000760"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14116"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13638"],["dc.identifier.url","https://sfb1002.med.uni-goettingen.de/production/literature/publications/187"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/8"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation","SFB 1002: Modulatorische Einheiten bei Herzinsuffizienz"],["dc.relation","SFB 1002 | A06: Molekulare Grundlagen mitochondrialer Kardiomyopathien"],["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","2045-2322"],["dc.relation.workinggroup","RG Lehnart (Cellular Biophysics and Translational Cardiology Section)"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.relation.workinggroup","RG Schuldiner (Functional Genomics of Organelles)"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Mice lacking WRB reveal differential biogenesis requirements of tail-anchored proteins in vivo"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]
    Details DOI PMID PMC
  • 2014Journal Article
    [["dc.bibliographiccitation.artnumber","e85033"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Vilardi, Fabio"],["dc.contributor.author","Stephan, Milena"],["dc.contributor.author","Clancy, Anne"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2017-09-07T11:46:54Z"],["dc.date.available","2017-09-07T11:46:54Z"],["dc.date.issued","2014"],["dc.description.abstract","Tail-Anchored (TA) proteins are inserted into the endoplasmic reticulum (ER) membrane of yeast cells via the posttranslational Guided Entry of Tail-Anchored protein (GET) pathway. The key component of this targeting machinery is the ATPase Get3 that docks to the ER membrane by interacting with a receptor complex formed by the proteins Get1 and Get2. A conserved pathway is present in higher eukaryotes and is mediated by TRC40, homolog of Get3, and the recently identified membrane receptors WRB and CAML. Here, we used yeast lacking the GET1 and GET2 genes and substituted them with WRB and CAML. This rescued the growth phenotypes of the GET receptor mutant. We demonstrate that WRB and CAML efficiently recruit Get3 to the ER membrane and promote the targeting of the TA proteins in vivo. Our results show that the membrane spanning segments of CAML are essential to create a functional receptor with WRB and to ensure TA protein membrane insertion. Finally, we determined the binding parameters of TRC40 to the WRB/CAML receptor. We conclude that together, WRB and CAML are not only necessary but also sufficient to create a functional membrane receptor complex for TRC40. The yeast complementation assay can be used to further dissect the structure-function relationship of the WRB/CAML heteromultimer in the absence of endogenous receptor proteins."],["dc.description.sponsorship","Open-Access-Publikatinsfonds 2014"],["dc.identifier.doi","10.1371/journal.pone.0085033"],["dc.identifier.gro","3142201"],["dc.identifier.isi","000329460100086"],["dc.identifier.pmid","24392163"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9662"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/5654"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: University Medicine Gottingen"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","1932-6203"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","WRB and CAML Are Necessary and Sufficient to Mediate Tail-Anchored Protein Targeting to the ER Membrane"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]
    Details DOI PMID PMC WOS