Neumann, Daniel

[["dc.bibliographiccitation.firstpage","1"],["dc.bibliographiccitation.lastpage","19"],["dc.bibliographiccitation.seriesnr","124"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Stoldt, Stefan"],["dc.contributor.author","Neumann, Daniel"],["dc.contributor.editor","Müller, Susann"],["dc.contributor.editor","Bley, Thomas"],["dc.date.accessioned","2017-09-07T11:45:03Z"],["dc.date.available","2017-09-07T11:45:03Z"],["dc.date.issued","2011"],["dc.description.abstract","Heterogeneity in the shapes of individual multicellular organisms is a daily experience. Likewise, even a quick glance through the ocular of a light microscope reveals the morphological heterogeneities in genetically identical cultured cells, whereas heterogeneities on the level of the organelles are much less obvious. This short review focuses on intracellular heterogeneities at the example of the mitochondria and their analysis by fluorescence microscopy. The overall mitochondrial shape as well as mitochondrial dynamics can be studied by classical (fluorescence) light microscopy. However, with an organelle diameter generally close to the resolution limit of light, the heterogeneities within mitochondria cannot be resolved with conventional light microscopy. Therefore, we briefly discuss here the potential of subdiffraction light microscopy (nanoscopy) to study inner-mitochondrial heterogeneities."],["dc.identifier.doi","10.1007/10_2010_81"],["dc.identifier.gro","3142799"],["dc.identifier.isi","000288919400001"],["dc.identifier.pmid","21072702"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/243"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Springer"],["dc.publisher.place","Berlin"],["dc.relation.crisseries","Advances in Biochemical Engineering, Biotechnology"],["dc.relation.isbn","978-3-642-16886-4"],["dc.relation.ispartof","High Resolution Microbial Single Cell Analytics"],["dc.relation.ispartofseries","Advances in Biochemical Engineering, Biotechnology; 124"],["dc.relation.issn","0724-6145"],["dc.relation.issn","0724-6145"],["dc.title","Light Microscopic Analysis of Mitochondrial Heterogeneity in Cell Populations and Within Single Cells"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","185"],["dc.bibliographiccitation.lastpage","199"],["dc.bibliographiccitation.seriesnr","591"],["dc.contributor.author","Wurm, Christian Andreas"],["dc.contributor.author","Neumann, Daniel"],["dc.contributor.author","Schmidt, Christoph"],["dc.contributor.author","Egner, Alexander"],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2017-09-07T11:53:08Z"],["dc.date.available","2017-09-07T11:53:08Z"],["dc.date.issued","2009"],["dc.identifier.doi","10.1007/978-1-60761-404-3_11"],["dc.identifier.gro","3145045"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2738"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.status","final"],["dc.publisher","Springer Nature"],["dc.relation.crisseries","Methods in Molecular Biology"],["dc.relation.isbn","978-1-60761-403-6"],["dc.relation.ispartof","Live Cell Imaging: Methods and Protocols"],["dc.relation.ispartofseries","Methods in Molecular Biology; 591"],["dc.relation.issn","1064-3745"],["dc.title","Sample Preparation for STED Microscopy"],["dc.type","book_chapter"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","13546"],["dc.bibliographiccitation.issue","33"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","13551"],["dc.bibliographiccitation.volume","108"],["dc.contributor.author","Wurm, Christian Andreas"],["dc.contributor.author","Neumann, Daniel"],["dc.contributor.author","Lauterbach, Marcel A."],["dc.contributor.author","Harke, Benjamin"],["dc.contributor.author","Egner, Alexander"],["dc.contributor.author","Hell, Stefan"],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2017-09-07T11:43:26Z"],["dc.date.available","2017-09-07T11:43:26Z"],["dc.date.issued","2011"],["dc.description.abstract","The translocase of the mitochondrial outer membrane (TOM) complex is the main import pore for nuclear-encoded proteins into mitochondria, yet little is known about its spatial distribution within the outer membrane. Super-resolution stimulated emission depletion microscopy was used to determine quantitatively the nanoscale distribution of Tom20, a subunit of the TOM complex, in more than 1,000 cells. We demonstrate that Tom20 is located in clusters whose nanoscale distribution is finely adjusted to the cellular growth conditions as well as to the specific position of a cell within a microcolony. The density of the clusters correlates to the mitochondrial membrane potential. The distributions of clusters of Tom20 and of Tom22 follow an inner-cellular gradient from the perinuclear to the peripheral mitochondria. We conclude that the nanoscale distribution of the TOM complex is finely adjusted to the cellular conditions, resulting in distribution gradients both within single cells and between adjacent cells."],["dc.identifier.doi","10.1073/pnas.1107553108"],["dc.identifier.gro","3142687"],["dc.identifier.isi","000293895100042"],["dc.identifier.pmid","21799113"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/118"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Nanoscale distribution of mitochondrial import receptor Tom20 is adjusted to cellular conditions and exhibits an inner-cellular gradient"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["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.firstpage","119"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","130"],["dc.bibliographiccitation.volume","181"],["dc.contributor.author","Altmann, Katrin"],["dc.contributor.author","Frank, Martina"],["dc.contributor.author","Neumann, Daniel"],["dc.contributor.author","Jakobs, Stefan"],["dc.contributor.author","Westermann, Benedikt"],["dc.date.accessioned","2017-09-07T11:48:45Z"],["dc.date.available","2017-09-07T11:48:45Z"],["dc.date.issued","2008"],["dc.description.abstract","The actin cytoskeleton is essential for polarized, bud-directed movement of cellular membranes in Saccharomyces cerevisiae and thus ensures accurate inheritance of organelles during cell division. Also, mitochondrial distribution and inheritance depend on the actin cytoskeleton, though the precise molecular mechanisms are unknown. Here, we establish the class V myosin motor protein, Myo2, as an important mediator of mitochondrial motility in budding yeast. We found that mutants with abnormal expression levels of Myo2 or its associated light chain, Mlc1, exhibit aberrant mitochondrial morphology and loss of mitochondrial DNA. Specific mutations in the globular tail of Myo2 lead to aggregation of mitochondria in the mother cell. Isolated mitochondria lacking functional Myo2 are severely impaired in their capacity to bind to actin. laments in vitro. Time-resolved. uorescence microscopy revealed a block of bud-directed anterograde mitochondrial movement in cargo binding-defective myo2 mutant cells. We conclude that Myo2 plays an important and direct role for mitochondrial motility and inheritance in budding yeast."],["dc.identifier.doi","10.1083/jcb.200709099"],["dc.identifier.gro","3143317"],["dc.identifier.isi","000254746500013"],["dc.identifier.pmid","18391073"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/818"],["dc.language.iso","en"],["dc.notes.intern","WoS Import 2017-03-10"],["dc.notes.status","final"],["dc.notes.submitter","PUB_WoS_Import"],["dc.relation.issn","0021-9525"],["dc.title","The class V myosin motor protein, Myo2, plays a major role in mitochondrial motility in Saccharomyces cerevisiae"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","4"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","PMC Biophysics"],["dc.bibliographiccitation.volume","3"],["dc.contributor.author","Neumann, Daniel"],["dc.contributor.author","Bückers, Johanna"],["dc.contributor.author","Kastrup, Lars"],["dc.contributor.author","Hell, Stefan W."],["dc.contributor.author","Jakobs, Stefan"],["dc.date.accessioned","2017-09-07T11:53:08Z"],["dc.date.available","2017-09-07T11:53:08Z"],["dc.date.issued","2010"],["dc.description.abstract","The voltage-dependent anion channel (VDAC, also known as mitochondrial porin) is the major transport channel mediating the transport of metabolites, including ATP, across the mitochondrial outer membrane. Biochemical data demonstrate the binding of the cytosolic protein hexokinase-I to VDAC, facilitating the direct access of hexokinase-I to the transported ATP. In human cells, three hVDAC isoforms have been identified. However, little is known on the distribution of these isoforms within the outer membrane of mitochondria and to what extent they colocalize with hexokinase- I. In this study we show that whereas hVDAC1 and hVDAC2 are localized predominantly within the same distinct domains in the outer membrane, hVDAC3 is mostly uniformly distributed over the surface of the mitochondrion. We used twocolor stimulated emission depletion (STED) microscopy enabling a lateral resolution of ~40 nm to determine the detailed sub-mitochondrial distribution of the three hVDAC isoforms and hexokinase-I. Individual hVDAC and hexokinase-I clusters could thus be resolved which were concealed in the confocal images. Quantitative colocalization analysis of two-color STED images demonstrates that within the attained resolution, hexokinase-I and hVDAC3 exhibit a higher degree of colocalization than hexokinase-I with either hVDAC1 or hVDAC2. Furthermore, a substantial fraction of the mitochondria-bound hexokinase-I pool does not colocalize with any of the three hVDAC isoforms, suggesting a more complex interplay of these proteins than previously anticipated. This study demonstrates that two-color STED microscopy in conjunction with quantitative colocalization analysis is a powerful tool to study the complex distribution of membrane proteins in organelles such as mitochondria."],["dc.identifier.doi","10.1186/1757-5036-3-4"],["dc.identifier.gro","3145044"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/5690"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/2737"],["dc.language.iso","en"],["dc.notes.intern","Crossref Import"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.issn","1757-5036"],["dc.rights","CC BY 2.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.0"],["dc.title","Two-color STED microscopy reveals different degrees of colocalization between hexokinase-I and the three human VDAC isoforms"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]