Simons, Mikael

[["dc.bibliographiccitation.firstpage","277"],["dc.bibliographiccitation.issue","1-2"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","290"],["dc.bibliographiccitation.volume","156"],["dc.contributor.author","Snaidero, Nicolas"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Czopka, Tim"],["dc.contributor.author","Hekking, Liesbeth H. P."],["dc.contributor.author","Mathisen, Cliff"],["dc.contributor.author","Verkleij, Dick"],["dc.contributor.author","Goebbels, Sandra"],["dc.contributor.author","Edgar, Julia M."],["dc.contributor.author","Merkler, Doron"],["dc.contributor.author","Lyons, David A."],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2018-11-07T09:45:05Z"],["dc.date.available","2018-11-07T09:45:05Z"],["dc.date.issued","2014"],["dc.description.abstract","Central nervous system myelin is a multilayered membrane sheath generated by oligodendrocytes for rapid impulse propagation. However, the underlying mechanisms of myelin wrapping have remained unclear. Using an integrative approach of live imaging, electron microscopy, and genetics, we show that new myelin membranes are incorporated adjacent to the axon at the innermost tongue. Simultaneously, newly formed layers extend laterally, ultimately leading to the formation of a set of closely apposed paranodal loops. An elaborated system of cytoplasmic channels within the growing myelin sheath enables membrane trafficking to the leading edge. Most of these channels close with ongoing development but can be reopened in adults by experimentally raising phosphatidylinositol-(3,4,5)-triphosphate levels, which reinitiates myelin growth. Our model can explain assembly of myelin as a multilayered structure, abnormal myelin outfoldings in neurological disease, and plasticity of myelin biogenesis observed in adult life."],["dc.identifier.doi","10.1016/j.cell.2013.11.044"],["dc.identifier.isi","000329912200027"],["dc.identifier.pmid","24439382"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/34540"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","1097-4172"],["dc.relation.issn","0092-8674"],["dc.title","Myelin Membrane Wrapping of CNS Axons by PI(3,4,5) P3-Dependent Polarized Growth at the Inner Tongue"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","2123"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","4"],["dc.contributor.author","Grapp, Marcel"],["dc.contributor.author","Wrede, Arne"],["dc.contributor.author","Schweizer, Michaela"],["dc.contributor.author","Huewel, Sabine"],["dc.contributor.author","Galla, Hans-Joachim"],["dc.contributor.author","Snaidero, Nicolas"],["dc.contributor.author","Simons, Mikael"],["dc.contributor.author","Bueckers, Johanna"],["dc.contributor.author","Low, Philip S."],["dc.contributor.author","Urlaub, Henning"],["dc.contributor.author","Gärtner, Jutta"],["dc.contributor.author","Steinfeld, Robert"],["dc.date.accessioned","2017-09-07T11:47:39Z"],["dc.date.available","2017-09-07T11:47:39Z"],["dc.date.issued","2013"],["dc.description.abstract","Loss of folate receptor-alpha function is associated with cerebral folate transport deficiency and childhood-onset neurodegeneration. To clarify the mechanism of cerebral folate transport at the blood-cerebrospinal fluid barrier, we investigate the transport of 5-methyltetrahydrofolate in polarized cells. Here we identify folate receptor-alpha-positive intralumenal vesicles within multivesicular bodies and demonstrate the directional cotransport of human folate receptor-alpha, and labelled folate from the basolateral to the apical membrane in rat choroid plexus cells. Both the apical medium of folate receptor-alpha-transfected rat choroid plexus cells and human cerebrospinal fluid contain folate receptor-alpha-positive exosomes. Loss of folate receptor-alpha-expressing cerebrospinal fluid exosomes correlates with severely reduced 5-methyltetrahydrofolate concentration, corroborating the importance of the folate receptor-alpha-mediated folate transport in the cerebrospinal fluid. Intraventricular injections of folate receptor-alpha-positive and -negative exosomes into mouse brains demonstrate folate receptor-alpha-dependent delivery of exosomes into the brain parenchyma. Our results unravel a new pathway of folate receptor-alpha-dependent exosome-mediated folate delivery into the brain parenchyma and opens new avenues for cerebral drug targeting."],["dc.identifier.doi","10.1038/ncomms3123"],["dc.identifier.gro","3142330"],["dc.identifier.isi","000323715900003"],["dc.identifier.pmid","23828504"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9774"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/7086"],["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.publisher","Nature Publishing Group"],["dc.relation.issn","2041-1723"],["dc.rights","Goescholar"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.title","Choroid plexus transcytosis and exosome shuttling deliver folate into brain parenchyma"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.subtype","original"],["dc.type.version","submitted_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1001577"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","PLoS Biology"],["dc.bibliographiccitation.volume","11"],["dc.contributor.author","Aggarwal, Shweta"],["dc.contributor.author","Snaidero, Nicolas"],["dc.contributor.author","Paehler, Gesa"],["dc.contributor.author","Frey, Steffen"],["dc.contributor.author","Sanchez, Paula"],["dc.contributor.author","Zweckstetter, Markus"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Schneider, Anja"],["dc.contributor.author","Weil, Marie-Theres"],["dc.contributor.author","Schaap, Iwan Alexander Taco"],["dc.contributor.author","Goerlich, Dirk"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2018-11-07T09:23:52Z"],["dc.date.available","2018-11-07T09:23:52Z"],["dc.date.issued","2013"],["dc.description.abstract","Rapid conduction of nerve impulses requires coating of axons by myelin. To function as an electrical insulator, myelin is generated as a tightly packed, lipid-rich multilayered membrane sheath. Knowledge about the mechanisms that govern myelin membrane biogenesis is required to understand myelin disassembly as it occurs in diseases such as multiple sclerosis. Here, we show that myelin basic protein drives myelin biogenesis using weak forces arising from its inherent capacity to phase separate. The association of myelin basic protein molecules to the inner leaflet of the membrane bilayer induces a phase transition into a cohesive mesh-like protein network. The formation of this protein network shares features with amyloid fibril formation. The process is driven by phenylalanine-mediated hydrophobic and amyloid-like interactions that provide the molecular basis for protein extrusion and myelin membrane zippering. These findings uncover a physicochemical mechanism of how a cytosolic protein regulates the morphology of a complex membrane architecture. These results provide a key mechanism in myelin membrane biogenesis with implications for disabling demyelinating diseases of the central nervous system."],["dc.description.sponsorship","ERC Starting Grant; German Research Foundation [SI 746/9-1, TRR43]"],["dc.identifier.doi","10.1371/journal.pbio.1001577"],["dc.identifier.fs","600727"],["dc.identifier.isi","000321042900005"],["dc.identifier.pmid","23762018"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9108"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/29688"],["dc.notes.intern","Merged from goescholar"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","1545-7885"],["dc.relation.orgunit","Fakultät für Physik"],["dc.rights","CC BY-NC-ND 3.0"],["dc.rights.uri","http://creativecommons.org/licenses/by-nc-nd/3.0/"],["dc.title","Myelin Membrane Assembly Is Driven by a Phase Transition of Myelin Basic Proteins Into a Cohesive Protein Meshwork"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","445"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","Developmental Cell"],["dc.bibliographiccitation.lastpage","456"],["dc.bibliographiccitation.volume","21"],["dc.contributor.author","Aggarwal, Shweta"],["dc.contributor.author","Yurlova, Larisa"],["dc.contributor.author","Snaidero, Nicolas"],["dc.contributor.author","Reetz, Christina"],["dc.contributor.author","Frey, Steffen"],["dc.contributor.author","Zimmermann, Johannes"],["dc.contributor.author","Paehler, Gesa"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Friedrichs, Jens"],["dc.contributor.author","Mueller, Daniel J."],["dc.contributor.author","Goebel, Cornelia"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2018-11-07T08:51:45Z"],["dc.date.available","2018-11-07T08:51:45Z"],["dc.date.issued","2011"],["dc.description.abstract","The insulating layers of myelin membrane wrapped around axons by oligodendrocytes are essential for the rapid conduction of nerve impulses in the central nervous system. To fulfill this function as an electrical insulator, myelin requires a unique lipid and protein composition. Here we show that oligodendrocytes employ a barrier that functions as a physical filter to generate the lipid-rich myelin-membrane sheets. Myelin basic protein (MBP) forms this molecular sieve and restricts the diffusion of proteins with large cytoplasmic domains into myelin. The barrier is generated from MBP molecules that line the entire sheet and is, thus, intimately intertwined with the biogenesis of the polarized cell surface. This system might have evolved in oligodendrocytes in order to generate an anisotropic membrane organization that facilitates the assembly of highly insulating lipid-rich membranes."],["dc.identifier.doi","10.1016/j.devcel.2011.08.001"],["dc.identifier.isi","000295060900010"],["dc.identifier.pmid","21885353"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/22011"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Cell Press"],["dc.relation.issn","1534-5807"],["dc.title","A Size Barrier Limits Protein Diffusion at the Cell Surface to Generate Lipid-Rich Myelin-Membrane Sheets"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","1146"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids"],["dc.bibliographiccitation.lastpage","1153"],["dc.bibliographiccitation.volume","1821"],["dc.contributor.author","Simons, Mikael"],["dc.contributor.author","Snaidero, Nicolas"],["dc.contributor.author","Aggarwal, Shweta"],["dc.date.accessioned","2018-11-07T09:08:06Z"],["dc.date.available","2018-11-07T09:08:06Z"],["dc.date.issued","2012"],["dc.description.abstract","Myelin-forming glia are highly polarized cells that synthesize as an extension of their plasma membrane, a multilayered myelin membrane sheath, with a unique protein and lipid composition. In most cells polarity is established by the polarized exocytosis of membrane vesicles to the distinct plasma membrane domains. Since myelin is composed of a stack of tightly packed membrane layers that do not leave sufficient space for the vesicular trafficking, we hypothesize that myelin does not use polarized exocytosis as a primary mechanism, but rather depends on lateral transport of membrane components in the plasma membrane. We suggest a model in which vesicle-mediated transport is confined to the cytoplasmic channels, from where transport to the compacted areas occurs by lateral flow of cargo within the plasma membrane. A diffusion barrier that is formed by MBP and the two adjacent cytoplasmic leaflets of the myelin bilayers acts a molecular sieve and regulates the flow of the components. Finally, we highlight potential mechanism that may contribute to the assembly of specific lipids within myelin. This article is part of a Special Issue entitled Lipids and Vesicular Transport. (C) 2012 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.bbalip.2012.01.011"],["dc.identifier.isi","000305847900012"],["dc.identifier.pmid","22314181"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/25949"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","1388-1981"],["dc.title","Cell polarity in myelinating glia: From membrane flow to diffusion barriers"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.artnumber","e1003980"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","PLoS Genetics"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Ghosh, Aniket"],["dc.contributor.author","Kling, Tina"],["dc.contributor.author","Snaidero, Nicolas"],["dc.contributor.author","Sampaio, Julio L."],["dc.contributor.author","Shevchenko, Andrej"],["dc.contributor.author","Gras, Heribert"],["dc.contributor.author","Geurten, Bart R. H."],["dc.contributor.author","Göpfert, Martin C."],["dc.contributor.author","Schulz, Joerg B."],["dc.contributor.author","Voigt, Aaron"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2018-11-07T09:16:43Z"],["dc.date.available","2018-11-07T09:16:43Z"],["dc.date.issued","2013"],["dc.description.abstract","Glia are of vital importance for all complex nervous system. One of the many functions of glia is to insulate and provide trophic and metabolic support to axons. Here, using glial-specific RNAi knockdown in Drosophila, we silenced 6930 conserved genes in adult flies to identify essential genes and pathways. Among our screening hits, metabolic processes were highly represented, and genes involved in carbohydrate and lipid metabolic pathways appeared to be essential in glia. One critical pathway identified was de novo ceramide synthesis. Glial knockdown of lace, a subunit of the serine palmitoyltransferase associated with hereditary sensory and autonomic neuropathies in humans, resulted in ensheathment defects of peripheral nerves in Drosophila. A genetic dissection study combined with shotgun high-resolution mass spectrometry of lipids showed that levels of ceramide phosphoethanolamine are crucial for axonal ensheathment by glia. A detailed morphological and functional analysis demonstrated that the depletion of ceramide phosphoethanolamine resulted in axonal defasciculation, slowed spike propagation, and failure of wrapping glia to enwrap peripheral axons. Supplementing sphingosine into the diet rescued the neuropathy in flies. Thus, our RNAi study in Drosophila identifies a key role of ceramide phosphoethanolamine in wrapping of axons by glia."],["dc.identifier.doi","10.1371/journal.pgen.1003980"],["dc.identifier.isi","000330533300023"],["dc.identifier.pmid","24348263"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/9570"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/27999"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Public Library Science"],["dc.relation.issn","1553-7404"],["dc.rights","CC BY 2.5"],["dc.rights.uri","https://creativecommons.org/licenses/by/2.5"],["dc.title","A Global In Vivo Drosophila RNAi Screen Identifies a Key Role of Ceramide Phosphoethanolamine for Glial Ensheathment of Axons"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","314"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Cell Reports"],["dc.bibliographiccitation.lastpage","323"],["dc.bibliographiccitation.volume","18"],["dc.contributor.author","Snaidero, Nicolas"],["dc.contributor.author","Velte, Caroline"],["dc.contributor.author","Myllykoski, Matti"],["dc.contributor.author","Raasakka, Arne"],["dc.contributor.author","Ignatev, Alexander"],["dc.contributor.author","Werner, Hauke B."],["dc.contributor.author","Erwig, Michelle S."],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Kursula, Petri"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2019-07-09T11:43:19Z"],["dc.date.available","2019-07-09T11:43:19Z"],["dc.date.issued","2017"],["dc.description.abstract","The myelin sheath is a multilamellar plasma membrane extension of highly specialized glial cells laid down in regularly spaced segments along axons. Recent studies indicate that myelin is metabolically active and capable of communicating with the underlying axon. To be functionally connected to the neuron, oligodendrocytes maintain non-compacted myelin as cytoplasmic nanochannels. Here, we used high-pressure freezing for electron microscopy to study these cytoplasmic regions within myelin close to their native state. We identified 2,030-cyclic nucleotide 30-phosphodiesterase (CNP), an oligodendrocyte- specific protein previously implicated in the maintenance of axonal integrity, as an essential factor in generating and maintaining cytoplasm within the myelin compartment. We provide evidence that CNP directly associates with and organizes the actin cytoskeleton, thereby providing an intracellular strut that counteracts membrane compaction by myelin basic protein (MBP). Our study provides amolecular and structural framework for understanding how myelin maintains its cytoplasm to function as an active axon-glial unit."],["dc.identifier.doi","10.1016/j.celrep.2016.12.053"],["dc.identifier.pmid","28076777"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/14431"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/58862"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/647168/EU/Cell biology of myelin wrapping, plasticity and turnover/Myelination"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/269020/EU/The role of myelinating glia in preserving axon function/AXOGLIA"],["dc.relation","info:eu-repo/grantAgreement/EC/FP7/671048/EU/Myelinic nanochannels in neurodegenerative diseases/MyeliNANO"],["dc.relation.issn","2211-1247"],["dc.rights","CC BY-NC-ND 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by-nc-nd/4.0"],["dc.title","Antagonistic Functions of MBP and CNP Establish Cytosolic Channels in CNS Myelin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2999"],["dc.bibliographiccitation.issue","14"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","3004"],["dc.bibliographiccitation.volume","127"],["dc.contributor.author","Snaidero, Nicolas"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2018-11-07T09:37:40Z"],["dc.date.available","2018-11-07T09:37:40Z"],["dc.date.issued","2014"],["dc.description.abstract","The myelin sheath is a plasma membrane extension that is laid down in regularly spaced segments along axons of the nervous system. This process involves extensive changes in oligodendrocyte cell shape and membrane architecture. In this Cell Science at a Glance article and accompanying poster, we provide a model of how myelin of the central nervous system is wrapped around axons to form a tightly compacted, multilayered membrane structure. This model may not only explain how myelin is generated during brain development, but could also help us to understand myelin remodeling in adult life, which might serve as a form of plasticity for the fine-tuning of neuronal networks."],["dc.identifier.doi","10.1242/jcs.151043"],["dc.identifier.isi","000339329700002"],["dc.identifier.pmid","25024457"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/32894"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Company Of Biologists Ltd"],["dc.relation.issn","1477-9137"],["dc.relation.issn","0021-9533"],["dc.title","Myelination at a glance"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3143"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","3148"],["dc.bibliographiccitation.volume","110"],["dc.contributor.author","Bakhti, Mostafa"],["dc.contributor.author","Snaidero, Nicolas"],["dc.contributor.author","Schneider, David"],["dc.contributor.author","Aggarwal, Shweta"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Janshoff, Andreas"],["dc.contributor.author","Eckhardt, Matthias"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2018-11-07T09:28:05Z"],["dc.date.available","2018-11-07T09:28:05Z"],["dc.date.issued","2013"],["dc.description.abstract","During the development of the central nervous system (CNS), oligodendrocytes wrap their plasma membrane around axons to form a multilayered stack of tightly attached membranes. Although in-tracellular myelin compaction and the role of myelin basic protein has been investigated, the forces that mediate the close interaction of myelin membranes at their external surfaces are poorly understood. Such extensive bilayer-bilayer interactions are usually prevented by repulsive forces generated by the glycocalyx, a dense and confluent layer of large and negatively charged oligosaccharides. Here we investigate the molecular mechanisms underlying myelin adhesion and compaction in the CNS. We revisit the role of the proteolipid protein and analyze the contribution of oligosaccharides using cellular assays, biophysical tools, and transgenic mice. We observe that differentiation of oligodendrocytes is accompanied by a striking down-regulation of components of their glycocalyx. Both in vitro and in vivo experiments indicate that the adhesive properties of the proteolipid protein, along with the reduction of sialic acid residues from the cell surface, orchestrate myelin membrane adhesion and compaction in the CNS. We suggest that loss of electrostatic cell-surface repulsion uncovers weak and unspecific attractive forces in the bilayer that bring the extracellular surfaces of a membrane into close contact over long distances."],["dc.identifier.doi","10.1073/pnas.1220104110"],["dc.identifier.isi","000315954400104"],["dc.identifier.pmid","23382229"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/30690"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Natl Acad Sciences"],["dc.relation.issn","0027-8424"],["dc.title","Loss of electrostatic cell-surface repulsion mediates myelin membrane adhesion and compaction in the central nervous system"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Nature Communications"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Djannatian, Minou"],["dc.contributor.author","Timmler, Sebastian"],["dc.contributor.author","Arends, Martina"],["dc.contributor.author","Luckner, Manja"],["dc.contributor.author","Weil, Marie-Theres"],["dc.contributor.author","Alexopoulos, Ioannis"],["dc.contributor.author","Snaidero, Nicolas"],["dc.contributor.author","Schmid, Bettina"],["dc.contributor.author","Misgeld, Thomas"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Schifferer, Martina"],["dc.contributor.author","Peles, Elior"],["dc.contributor.author","Simons, Mikael"],["dc.date.accessioned","2019-11-14T10:54:01Z"],["dc.date.accessioned","2021-10-27T13:21:27Z"],["dc.date.available","2019-11-14T10:54:01Z"],["dc.date.available","2021-10-27T13:21:27Z"],["dc.date.issued","2019"],["dc.description.abstract","Central nervous system myelin is a multilayered membrane produced by oligodendrocytes to increase neural processing speed and efficiency, but the molecular mechanisms underlying axonal selection and myelin wrapping are unknown. Here, using combined morphological and molecular analyses in mice and zebrafish, we show that adhesion molecules of the paranodal and the internodal segment work synergistically using overlapping functions to regulate axonal interaction and myelin wrapping. In the absence of these adhesive systems, axonal recognition by myelin is impaired with myelin growing on top of previously myelinated fibers, around neuronal cell bodies and above nodes of Ranvier. In addition, myelin wrapping is disturbed with the leading edge moving away from the axon and in between previously formed layers. These data show how two adhesive systems function together to guide axonal ensheathment and myelin wrapping, and provide a mechanistic understanding of how the spatial organization of myelin is achieved."],["dc.identifier.doi","10.1038/s41467-019-12789-z"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/16665"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/92023"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.relation.eissn","2041-1723"],["dc.relation.issn","2041-1723"],["dc.relation.orgunit","Universitätsmedizin Göttingen"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.subject.ddc","573"],["dc.subject.ddc","612"],["dc.title","Two adhesive systems cooperatively regulate axon ensheathment and myelin growth in the CNS"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]