Wurm, Christian Andreas

[["dc.bibliographiccitation.firstpage","2292"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Molecular Biology of the Cell"],["dc.bibliographiccitation.lastpage","2301"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Stoldt, Stefan"],["dc.contributor.author","Wenzel, Dirk"],["dc.contributor.author","Hildenbeutel, Markus"],["dc.contributor.author","Wurm, Christian Andreas"],["dc.contributor.author","Herrmann, Johannes M."],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2017-09-07T11:48:51Z"],["dc.date.available","2017-09-07T11:48:51Z"],["dc.date.issued","2012"],["dc.description.abstract","The Oxa1 protein is a well-conserved integral protein of the inner membrane of mitochondria. It mediates the insertion of both mitochondrial-and nuclear-encoded proteins from the matrix into the inner membrane. We investigated the distribution of budding yeast Oxa1 between the two subdomains of the contiguous inner membrane-the cristae membrane (CM) and the inner boundary membrane (IBM)-under different physiological conditions. We found that under fermentable growth conditions, Oxa1 is enriched in the IBM, whereas under nonfermentable (respiratory) growth conditions, it is predominantly localized in the CM. The enrichment of Oxa1 in the CM requires mitochondrial translation; similarly, deletion of the ribosome-binding domain of Oxa1 prevents an enrichment of Oxa1 in the CM. The predominant localization in the IBM under fermentable growth conditions is prevented by inhibiting mitochondrial protein import. Furthermore, overexpression of the nuclear-encoded Oxa1 substrate Mdl1 shifts the distribution of Oxa1 toward the IBM. Apparently, the availability of nuclear- and mitochondrial-encoded substrates influences the inner-membrane distribution of Oxa1. Our findings show that the distribution of Oxa1 within the inner membrane is dynamic and adapts to different physiological needs."],["dc.identifier.doi","10.1091/mbc.E11-06-0538"],["dc.identifier.gro","3142518"],["dc.identifier.isi","000306286700006"],["dc.identifier.pmid","22513091"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9497"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/8878"],["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","1059-1524"],["dc.rights","CC BY-NC-SA 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-sa/3.0"],["dc.title","The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates"],["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","572"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Biology"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Bollmann, Franziska"],["dc.contributor.author","Dohrke, Jan-Niklas"],["dc.contributor.author","Wurm, Christian A."],["dc.contributor.author","Jans, Daniel C."],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2021-09-01T06:43:08Z"],["dc.date.available","2021-09-01T06:43:08Z"],["dc.date.issued","2021"],["dc.description.abstract","Mitochondria are highly dynamic organelles that interchange their contents mediated by fission and fusion. However, it has previously been shown that the mitochondria of cultured human epithelial cells exhibit a gradient in the relative abundance of several proteins, with the perinuclear mitochondria generally exhibiting a higher protein abundance than the peripheral mitochondria. The molecular mechanisms that are required for the establishment and the maintenance of such inner-cellular mitochondrial protein abundance gradients are unknown. We verified the existence of inner-cellular gradients in the abundance of clusters of the mitochondrial outer membrane protein Tom20 in the mitochondria of kidney epithelial cells from an African green monkey (Vero cells) using STED nanoscopy and confocal microscopy. We found that the Tom20 gradients are established immediately after cell division and require the presence of microtubules. Furthermore, the gradients are abrogated in hyperfused mitochondrial networks. Our results suggest that inner-cellular protein abundance gradients from the perinuclear to the peripheral mitochondria are established by the trafficking of individual mitochondria to their respective cellular destination."],["dc.description.abstract","Mitochondria are highly dynamic organelles that interchange their contents mediated by fission and fusion. However, it has previously been shown that the mitochondria of cultured human epithelial cells exhibit a gradient in the relative abundance of several proteins, with the perinuclear mitochondria generally exhibiting a higher protein abundance than the peripheral mitochondria. The molecular mechanisms that are required for the establishment and the maintenance of such inner-cellular mitochondrial protein abundance gradients are unknown. We verified the existence of inner-cellular gradients in the abundance of clusters of the mitochondrial outer membrane protein Tom20 in the mitochondria of kidney epithelial cells from an African green monkey (Vero cells) using STED nanoscopy and confocal microscopy. We found that the Tom20 gradients are established immediately after cell division and require the presence of microtubules. Furthermore, the gradients are abrogated in hyperfused mitochondrial networks. Our results suggest that inner-cellular protein abundance gradients from the perinuclear to the peripheral mitochondria are established by the trafficking of individual mitochondria to their respective cellular destination."],["dc.description.sponsorship","Deutsche Forschungsgemeinschaft"],["dc.description.sponsorship","European Research Council"],["dc.identifier.doi","10.3390/biology10070572"],["dc.identifier.pii","biology10070572"],["dc.identifier.pmid","34201436"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/89225"],["dc.identifier.url","https://sfb1190.med.uni-goettingen.de/production/literature/publications/146"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-455"],["dc.relation","SFB 1190: Transportmaschinen und Kontaktstellen zellulärer Kompartimente"],["dc.relation","SFB 1190 | P01: Untersuchung der Unterschiede in der Zusammensetzung, Funktion und Position von individuellen MICOS Komplexen in einzelnen Säugerzellen"],["dc.relation.eissn","2079-7737"],["dc.relation.workinggroup","RG Jakobs (Structure and Dynamics of Mitochondria)"],["dc.rights","https://creativecommons.org/licenses/by/4.0/"],["dc.title","Mitochondrial Protein Abundance Gradients Require the Distribution of Separated Mitochondria"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.subtype","original_ja"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","7"],["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Optical Nanoscopy"],["dc.bibliographiccitation.lastpage","7"],["dc.bibliographiccitation.volume","1"],["dc.contributor.author","Wurm, Christian Andreas"],["dc.contributor.author","Kolmakov, Kirill"],["dc.contributor.author","Göttfert, Fabian"],["dc.contributor.author","Ta, Haisen"],["dc.contributor.author","Bossi, Mariano"],["dc.contributor.author","Schill, Heiko"],["dc.contributor.author","Berning, Sebastian"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Donnert, Gerald"],["dc.contributor.author","Belov, Vladimir N."],["dc.contributor.author","Hell, Stefan W."],["dc.date.accessioned","2017-09-07T11:53:03Z"],["dc.date.available","2017-09-07T11:53:03Z"],["dc.date.issued","2012"],["dc.description.abstract","In optical microscopy, most red-emitting dyes provide only moderate performance due to unspecific binding, poor labeling efficiency, and insufficient brightness. Here we report on four novel red fluororescent dyes, including the first phosphorylated dye, created by combining a rigidized rhodamine backbone with various polar groups. They exhibit large fluorescence quantum yields and improved NHS ester stability. While these fluorophores are highly suitable for fluorescence microscopy in general, they excel in stimulated emission depletion (STED) microscopy, providing < 25 nm spatial resolution in raw images of cells."],["dc.identifier.doi","10.1186/2192-2853-1-7"],["dc.identifier.fs","593636"],["dc.identifier.gro","3145019"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/8898"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2709"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.issn","2192-2853"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","Goescholar"],["dc.rights.uri","https://goedoc.uni-goettingen.de/licenses"],["dc.title","Novel red fluorophores with superior performance in STED microscopy"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","no"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","402"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","EMBO Journal"],["dc.bibliographiccitation.lastpage","413"],["dc.bibliographiccitation.volume","35"],["dc.contributor.author","Große, Lena"],["dc.contributor.author","Wurm, Christian Andreas"],["dc.contributor.author","Brüser, Christian"],["dc.contributor.author","Neumann, Daniel"],["dc.contributor.author","Jans, Daniel C."],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2017-09-07T11:54:38Z"],["dc.date.available","2017-09-07T11:54:38Z"],["dc.date.issued","2016"],["dc.description.abstract","The Bcl-2 family proteins Bax and Bak are essential for the execution of many apoptotic programs. During apoptosis, Bax translocates to the mitochondria and mediates the permeabilization of the outer membrane, thereby facilitating the release of pro-apoptotic proteins. Yet the mechanistic details of the Bax-induced membrane permeabilization have so far remained elusive. Here, we demonstrate that activated Bax molecules, besides forming large and compact clusters, also assemble, potentially with other proteins including Bak, into ring-like structures in the mitochondrial outer membrane. STED nanoscopy indicates that the area enclosed by a Bax ring is devoid of mitochondrial outer membrane proteins such as Tom20, Tom22, and Sam50. This strongly supports the view that the Bax rings surround an opening required for mitochondrial outer membrane permeabilization (MOMP). Even though these Bax assemblies may be necessary for MOMP, we demonstrate that at least in Drp1 knockdown cells, these assemblies are not sufficient for full cytochrome c release. Together, our super-resolution data provide direct evidence in support of large Bax-delineated pores in the mitochondrial outer membrane as being crucial for Bax-mediated MOMP in cells."],["dc.identifier.doi","10.15252/embj.201592789"],["dc.identifier.gro","3141728"],["dc.identifier.isi","000370346400005"],["dc.identifier.pmid","26783364"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14032"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/413"],["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","1460-2075"],["dc.relation.issn","0261-4189"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Bax assembles into large ring-like structures remodeling the mitochondrial outer membrane in apoptosis"],["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.artnumber","e101563"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","PLOS ONE"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Ilgen, Peter"],["dc.contributor.author","Stoldt, Stefan"],["dc.contributor.author","Conradi, Lena-Christin"],["dc.contributor.author","Wurm, Christian Andreas"],["dc.contributor.author","Rüschoff, Josef"],["dc.contributor.author","Ghadimi, B. Michael"],["dc.contributor.author","Liersch, Torsten"],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2017-09-07T11:45:42Z"],["dc.date.available","2017-09-07T11:45:42Z"],["dc.date.issued","2014"],["dc.description.abstract","Formalin fixed and paraffin-embedded human tissue resected during cancer surgery is indispensable for diagnostic and therapeutic purposes and represents a vast and largely unexploited resource for research. Optical microscopy of such specimen is curtailed by the diffraction-limited resolution of conventional optical microscopy. To overcome this limitation, we used STED super-resolution microscopy enabling optical resolution well below the diffraction barrier. We visualized nanoscale protein distributions in sections of well-annotated paraffin-embedded human rectal cancer tissue stored in a clinical repository. Using antisera against several mitochondrial proteins, STED microscopy revealed distinct sub-mitochondrial protein distributions, suggesting a high level of structural preservation. Analysis of human tissues stored for up to 17 years demonstrated that these samples were still amenable for super-resolution microscopy. STED microscopy of sections of HER2 positive rectal adenocarcinoma revealed details in the surface and intracellular HER2 distribution that were blurred in the corresponding conventional images, demonstrating the potential of super-resolution microscopy to explore the thus far largely untapped nanoscale regime in tissues stored in biorepositories."],["dc.description.sponsorship","Open-Access-Publikationsfonds 2014"],["dc.identifier.doi","10.1371/journal.pone.0101563"],["dc.identifier.gro","3142087"],["dc.identifier.isi","000339992400018"],["dc.identifier.pmid","25025184"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/10481"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4400"],["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 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","STED Super-Resolution Microscopy of Clinical Paraffin-Embedded Human Rectal Cancer Tissue"],["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.artnumber","e78745"],["dc.bibliographiccitation.issue","10"],["dc.bibliographiccitation.journal","PLOS ONE"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Stagge, Franziska"],["dc.contributor.author","Mitronova, Gyuzel Yu"],["dc.contributor.author","Belov, Vladimir N."],["dc.contributor.author","Wurm, Christian Andreas"],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2017-09-07T11:47:06Z"],["dc.date.available","2017-09-07T11:47:06Z"],["dc.date.issued","2013"],["dc.description.abstract","Fluorescence microscopy of the localization and the spatial and temporal dynamics of specifically labelled proteins is an indispensable tool in cell biology. Besides fluorescent proteins as tags, tag-mediated labelling utilizing self-labelling proteins as the SNAP-, CLIP-, or the Halo-tag are widely used, flexible labelling systems relying on exogenously supplied fluorophores. Unfortunately, labelling of live budding yeast cells proved to be challenging with these approaches because of the limited accessibility of the cell interior to the dyes. In this study we developed a fast and reliable electroporation-based labelling protocol for living budding yeast cells expressing SNAP-, CLIP-, or Halo-tagged fusion proteins. For the Halo-tag, we demonstrate that it is crucial to use the 6'-carboxy isomers and not the 5'-carboxy isomers of important dyes to ensure cell viability. We report on a simple rule for the analysis of H-1 NMR spectra to discriminate between 6'- and 5'-carboxy isomers of fluorescein and rhodamine derivatives. We demonstrate the usability of the labelling protocol by imaging yeast cells with STED super-resolution microscopy and dual colour live cell microscopy. The large number of available fluorophores for these self-labelling proteins and the simplicity of the protocol described here expands the available toolbox for the model organism Saccharomyces cerevisiae."],["dc.identifier.doi","10.1371/journal.pone.0078745"],["dc.identifier.gro","3142268"],["dc.identifier.isi","000326155400102"],["dc.identifier.pmid","24205303"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9435"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/6398"],["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 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","Snap-, CLIP- and Halo-Tag Labelling of Budding Yeast Cells"],["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","9"],["dc.bibliographiccitation.journal","Current Opinion in Chemical Biology"],["dc.bibliographiccitation.lastpage","15"],["dc.bibliographiccitation.volume","20"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Wurm, Christian Andreas"],["dc.date.accessioned","2017-09-07T11:46:12Z"],["dc.date.available","2017-09-07T11:46:12Z"],["dc.date.issued","2014"],["dc.description.abstract","Mitochondria, the powerhouses of the cell, are essential organelles in eukaryotic cells. With their complex inner architecture featuring a smooth outer and a highly convoluted inner membrane, they are challenging objects for microscopy. The diameter of mitochondria is generally close to the resolution limit of conventional light microscopy, rendering diffraction-unlimited super-resolution light microscopy (nanoscopy) for imaging submitochondrial protein distributions often mandatory. In this review, we discuss what can be expected when imaging mitochondria with conventional diffraction-limited and diffraction-unlimited microscopy. We provide an overview on recent studies using super-resolution microscopy to investigate mitochondria and discuss further developments and challenges in mitochondrial biology that might by addressed with these technologies in the future."],["dc.identifier.doi","10.1016/j.cbpa.2014.03.019"],["dc.identifier.gro","3142108"],["dc.identifier.isi","000347500100003"],["dc.identifier.pmid","24769752"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/11353"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/4633"],["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","1879-0402"],["dc.relation.issn","1367-5931"],["dc.rights","CC BY-NC-SA 3.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-sa/3.0"],["dc.title","Super-resolution microscopy of mitochondria"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]