Clancy, Anne

[["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","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","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.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"]]

[["dc.bibliographiccitation.artnumber","e59590"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","PLoS ONE"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Leznicki, Pawel"],["dc.contributor.author","Roebuck, Quentin P."],["dc.contributor.author","Wunderley, Lydia"],["dc.contributor.author","Clancy, Anne"],["dc.contributor.author","Krysztofinska, Ewelina M."],["dc.contributor.author","Isaacson, Rivka L."],["dc.contributor.author","Warwicker, Jim"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","High, Stephen"],["dc.date.accessioned","2017-09-07T11:47:44Z"],["dc.date.available","2017-09-07T11:47:44Z"],["dc.date.issued","2013"],["dc.description.abstract","Background: The BAG6 protein is a subunit of a heterotrimeric complex that binds a range of membrane and secretory protein precursors localized to the cytosol, enforcing quality control and influencing their subsequent fate. Methodology and Principal Findings: BAG6 has an N-terminal ubiquitin-like domain, and a C-terminal Bcl-2-associated athanogene domain, separated by a large central proline-rich region. We have used in vitro binding approaches to identify regions of BAG6 important for its interactions with: i) the small-glutamine rich tetratricopeptide repeat-containing protein alpha (SGTA) and ii) two model tail-anchored membrane proteins as a paradigm for its hydrophobic substrates. We show that the BAG6-UBL is essential for binding to SGTA, and find that the UBL of a second subunit of the BAG6-complex, ubiquitin-like protein 4A (UBL4A), competes for SGTA binding. Our data show that this binding is selective, and suggest that SGTA can bind either BAG6, or UBL4A, but not both at the same time. We adapted our in vitro binding assay to study the association of BAG6 with an immobilized tail-anchored protein, Sec61b, and find both the UBL and BAG domains are dispensable for binding this substrate. This conclusion was further supported using a heterologous subcellular localization assay in yeast, where the BAG6-dependent nuclear relocalization of a second tail-anchored protein, GFP-Sed5, also required neither the UBL, nor the BAG domain of BAG6. Significance: On the basis of these findings, we propose a working model where the large central region of the BAG6 protein provides a binding site for a diverse group of substrates, many of which expose a hydrophobic stretch of polypeptide. This arrangement would enable the BAG6 complex to bring together its substrates with potential effectors including those recruited via its N-terminal UBL. Such effectors may include SGTA, and the resulting assemblies influence the subsequent fate of the hydrophobic BAG6 substrates."],["dc.identifier.doi","10.1371/journal.pone.0059590"],["dc.identifier.gro","3142369"],["dc.identifier.isi","000316549400072"],["dc.identifier.pmid","23533635"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8748"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7519"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["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 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/3.0"],["dc.title","The Association of BAG6 with SGTA and Tail-Anchored Proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2170"],["dc.bibliographiccitation.issue","13"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","2178"],["dc.bibliographiccitation.volume","123"],["dc.contributor.author","Leznicki, Pawel"],["dc.contributor.author","Clancy, Anne"],["dc.contributor.author","Schwappach, Blanche"],["dc.contributor.author","High, Stephen"],["dc.date.accessioned","2017-09-07T11:45:57Z"],["dc.date.available","2017-09-07T11:45:57Z"],["dc.date.issued","2010"],["dc.description.abstract","The membrane integration of tail-anchored proteins at the endoplasmic reticulum (ER) is post-translational, with different tail-anchored proteins exploiting distinct cytosolic factors. For example, mammalian TRC40 has a well-defined role during delivery of tail-anchored proteins to the ER. Although its Saccharomyces cerevisiae equivalent, Get3, is known to function in concert with at least four other components, Get1, Get2, Get4 and Get5 (Mdy2), the role of additional mammalian proteins during tail-anchored protein biogenesis is unclear. To this end, we analysed the cytosolic binding partners of Sec61 beta, a well-defined substrate of TRC40, and identified Bat3 as a previously unknown interacting partner. Depletion of Bat3 inhibits the membrane integration of Sec61 beta, but not of a second, TRC40-independent, tail-anchored protein, cytochrome b5. Thus, Bat3 influences the in vitro membrane integration of tail-anchored proteins using the TRC40 pathway. When expressed in Saccharomyces cerevisiae lacking a functional GET pathway for tail-anchored protein biogenesis, Bat3 associates with the resulting cytosolic pool of non-targeted chains and diverts it to the nucleus. This Bat3-mediated mislocalisation is not dependent upon Sgt2, a recently identified component of the yeast GET pathway, and we propose that Bat3 either modulates the TRC40 pathway in higher eukaryotes or provides an alternative fate for newly synthesised tail-anchored proteins."],["dc.identifier.doi","10.1242/jcs.066738"],["dc.identifier.gro","3142898"],["dc.identifier.isi","000278856400004"],["dc.identifier.pmid","20516149"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/353"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: Wellcome Trust"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1477-9137"],["dc.relation.issn","0021-9533"],["dc.title","Bat3 promotes the membrane integration of tail-anchored proteins"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["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"]]

[["dc.bibliographiccitation.firstpage","320"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","RNA Biology"],["dc.bibliographiccitation.lastpage","330"],["dc.bibliographiccitation.volume","13"],["dc.contributor.author","Heininger, Annika U."],["dc.contributor.author","Hackert, Phillip"],["dc.contributor.author","Andreou, Alexandra Z."],["dc.contributor.author","Boon, Kum-Loong"],["dc.contributor.author","Memet, Indira"],["dc.contributor.author","Prior, Mira"],["dc.contributor.author","Clancy, Anne"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Schleiff, Enrico"],["dc.contributor.author","Sloan, Katherine E."],["dc.contributor.author","Deckers, Markus"],["dc.contributor.author","Lührmann, Reinhard"],["dc.contributor.author","Enderlein, Jörg"],["dc.contributor.author","Klostermeier, Dagmar"],["dc.contributor.author","Rehling, Peter"],["dc.contributor.author","Bohnsack, Markus T."],["dc.date.accessioned","2017-09-07T11:54:35Z"],["dc.date.available","2017-09-07T11:54:35Z"],["dc.date.issued","2016"],["dc.description.abstract","A rapidly increasing number of RNA helicases are implicated in several distinct cellular processes, however, the modes of regulation of multifunctional RNA helicases and their recruitment to different target complexes have remained unknown. Here, we show that the distribution of the multifunctional DEAH-box RNA helicase Prp43 between its diverse cellular functions can be regulated by the interplay of its G-patch protein cofactors. We identify the orphan G-patch protein Cmg1 (YLR271W) as a novel cofactor of Prp43 and show that it stimulates the RNA binding and ATPase activity of the helicase. Interestingly, Cmg1 localizes to the cytoplasm and to the intermembrane space of mitochondria and its overexpression promotes apoptosis. Furthermore, our data reveal that different G-patch protein cofactors compete for interaction with Prp43. Changes in the expression levels of Prp43-interacting G-patch proteins modulate the cellular localization of Prp43 and G-patch protein overexpression causes accumulation of the helicase in the cytoplasm or nucleoplasm. Overexpression of several G-patch proteins also leads to defects in ribosome biogenesis that are consistent with withdrawal of the helicase from this pathway. Together, these findings suggest that the availability of cofactors and the sequestering of the helicase are means to regulate the activity of multifunctional RNA helicases and their distribution between different cellular processes."],["dc.description.sponsorship","Open-Access Publikationsfonds 2016"],["dc.identifier.doi","10.1080/15476286.2016.1142038"],["dc.identifier.gro","3141714"],["dc.identifier.isi","000372909600008"],["dc.identifier.pmid","26821976"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/13404"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/258"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.eissn","1555-8584"],["dc.relation.issn","1547-6286"],["dc.rights","CC BY-NC 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc/3.0"],["dc.title","Protein cofactor competition regulates the action of a multifunctional RNA helicase in different pathways"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","6916"],["dc.bibliographiccitation.issue","25"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","6921"],["dc.bibliographiccitation.volume","113"],["dc.contributor.author","Arakel, Eric C."],["dc.contributor.author","Richter, Kora P."],["dc.contributor.author","Clancy, Anne"],["dc.contributor.author","Schwappach, Blanche"],["dc.date.accessioned","2017-09-07T11:44:51Z"],["dc.date.available","2017-09-07T11:44:51Z"],["dc.date.issued","2016"],["dc.description.abstract","Membrane recruitment of coatomer and formation of coat protein I (COPI)-coated vesicles is crucial to homeostasis in the early secretory pathway. The conformational dynamics of COPI during cargo capture and vesicle formation is incompletely understood. By scanning the length of delta-COP via functional complementation in yeast, we dissect the domains of the delta-COP subunit. We show that the mu-homology domain is dispensable for COPI function in the early secretory pathway, whereas the N-terminal longin domain is essential. We map a previously uncharacterized helix, C-terminal to the longin domain, that is specifically required for the retrieval of HDEL-bearing endoplasmic reticulum-luminal residents. It is positionally analogous to an unstructured linker that becomes helical and membrane-facing in the open form of the AP2 clathrin adaptor complex. Based on the amphipathic nature of the critical helix it may probe the membrane for lipid packing defects or mediate interaction with cargo and thus contribute to stabilizing membrane-associated coatomer."],["dc.identifier.doi","10.1073/pnas.1603544113"],["dc.identifier.gro","3141664"],["dc.identifier.isi","000378272400043"],["dc.identifier.pmid","27298352"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6897"],["dc.notes.intern","WoS Import 2017-03-10 / Funder: University Medical Center Gottingen"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","delta-COP contains a helix C-terminal to its longin domain key to COPI dynamics and function"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","83"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","92"],["dc.bibliographiccitation.volume","216"],["dc.contributor.author","Schendzielorz, Alexander Benjamin"],["dc.contributor.author","Schulz, Christian"],["dc.contributor.author","Lytovchenko, Oleksandr"],["dc.contributor.author","Clancy, Anne"],["dc.contributor.author","Guiard, Bernard"],["dc.contributor.author","Ieva, Raffaele"],["dc.contributor.author","van der Laan, Martin"],["dc.contributor.author","Rehling, Peter"],["dc.date.accessioned","2017-09-07T11:53:21Z"],["dc.date.available","2017-09-07T11:53:21Z"],["dc.date.issued","2017"],["dc.description.abstract","wo driving forces energize precursor translocation across the inner mitochondrial membrane. Although the membrane potential (Δψ) is considered to drive translocation of positively charged presequences through the TIM23 complex (presequence translocase), the activity of the Hsp70-powered import motor is crucial for the translocation of the mature protein portion into the matrix. In this study, we show that mitochondrial matrix proteins display surprisingly different dependencies on the Δψ. However, a precursor's hypersensitivity to a reduction of the Δψ is not linked to the respective presequence, but rather to the mature portion of the polypeptide chain. The presequence translocase constituent Pam17 is specifically recruited by the receptor Tim50 to promote the transport of hypersensitive precursors into the matrix. Our analyses show that two distinct Δψ-driven translocation steps energize precursor passage across the inner mitochondrial membrane. The Δψ- and Pam17-dependent import step identified in this study is positioned between the two known energy-dependent steps: Δψ-driven presequence translocation and adenosine triphosphate-driven import motor activity."],["dc.identifier.doi","10.1083/jcb.201607066"],["dc.identifier.gro","3145078"],["dc.identifier.pmid","28011846"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2774"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/7"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["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","0021-9525"],["dc.relation.workinggroup","RG Rehling (Mitochondrial Protein Biogenesis)"],["dc.relation.workinggroup","RG Schwappach (Membrane Protein Biogenesis)"],["dc.rights","CC BY-NC-SA 4.0"],["dc.title","Two distinct membrane potential–dependent steps drive mitochondrial matrix protein translocation"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dc.type.subtype","original_ja"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]