Werner, Hauke B.

[["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","37"],["dc.bibliographiccitation.lastpage","63"],["dc.bibliographiccitation.seriesnr","1936"],["dc.contributor.author","Erwig, Michelle S."],["dc.contributor.author","Hesse, Dörte"],["dc.contributor.author","Jung, Ramona B."],["dc.contributor.author","Uecker, Marina"],["dc.contributor.author","Kusch, Kathrin"],["dc.contributor.author","Tenzer, Stefan"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Werner, Hauke B."],["dc.contributor.editor","Lyons, David A."],["dc.contributor.editor","Kegel, Linde"],["dc.date.accessioned","2021-06-02T10:44:26Z"],["dc.date.available","2021-06-02T10:44:26Z"],["dc.date.issued","2019"],["dc.identifier.doi","10.1007/978-1-4939-9072-6_3"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/87040"],["dc.notes.intern","DOI-Import GROB-425"],["dc.publisher","Springer New York"],["dc.publisher.place","New York, NY"],["dc.relation.crisseries","Methods in Molecular Biology"],["dc.relation.eisbn","978-1-4939-9072-6"],["dc.relation.isbn","978-1-4939-9070-2"],["dc.relation.ispartof","Methods in Molecular Biology"],["dc.relation.ispartof","Oligodendrocytes : Methods and Protocols"],["dc.relation.ispartofseries","Methods in Molecular Biology; 1936"],["dc.title","Myelin: Methods for Purification and Proteome Analysis"],["dc.type","book_chapter"],["dc.type.internalPublication","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","eLife"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Erwig, Michelle S."],["dc.contributor.author","Patzig, Julia"],["dc.contributor.author","Steyer, Anna M."],["dc.contributor.author","Dibaj, Payam"],["dc.contributor.author","Heilmann, Mareike"],["dc.contributor.author","Heilmann, Ingo"],["dc.contributor.author","Jung, Ramona B."],["dc.contributor.author","Kusch, Kathrin"],["dc.contributor.author","Möbius, Wiebke"],["dc.contributor.author","Jahn, Olaf"],["dc.contributor.author","Nave, Klaus-Armin"],["dc.contributor.author","Werner, Hauke B."],["dc.date.accessioned","2019-08-02T06:29:41Z"],["dc.date.available","2019-08-02T06:29:41Z"],["dc.date.issued","2019"],["dc.description.abstract","Myelin serves as an axonal insulator that facilitates rapid nerve conduction along axons. By transmission electron microscopy, a healthy myelin sheath comprises compacted membrane layers spiraling around the cross-sectioned axon. Previously we identified the assembly of septin filaments in the innermost non-compacted myelin layer as one of the latest steps of myelin maturation in the central nervous system (CNS) (Patzig et al., 2016). Here we show that loss of the cytoskeletal adaptor protein anillin (ANLN) from oligodendrocytes disrupts myelin septin assembly, thereby causing the emergence of pathological myelin outfoldings. Since myelin outfoldings are a poorly understood hallmark of myelin disease and brain aging we assessed axon/myelin-units in Anln-mutant mice by focused ion beam-scanning electron microscopy (FIB-SEM); myelin outfoldings were three-dimensionally reconstructed as large sheets of multiple compact membrane layers. We suggest that anillin-dependent assembly of septin filaments scaffolds mature myelin sheaths, facilitating rapid nerve conduction in the healthy CNS."],["dc.identifier.doi","10.7554/eLife.43888"],["dc.identifier.pmid","30672734"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/15932"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/62262"],["dc.language.iso","en"],["dc.notes.intern","Merged from goescholar"],["dc.notes.status","final"],["dc.relation.eissn","2050-084X"],["dc.relation.issn","2050-084X"],["dc.rights","CC BY 4.0"],["dc.rights.uri","https://creativecommons.org/licenses/by/4.0"],["dc.title","Anillin facilitates septin assembly to prevent pathological outfoldings of central nervous system myelin"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]