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Journal Article

Anillin facilitates septin assembly to prevent pathological outfoldings of central nervous system myelin

MPS-Authors
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Erwig,  Michelle S.
Neurogenetics, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Patzig,  Julia
Neurogenetics, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Steyer,  Anna M.
Neurogenetics, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Dibaj,  Payam
Neurogenetics, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Jung,  Ramona B.
Neurogenetics, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Kusch,  Kathrin
Neurogenetics, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Möbius,  Wiebke
Electron microscopy, Neurogenetics, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Jahn,  Olaf
Proteomics, Wiss. Servicegruppen, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Nave,  Klaus-Armin
Neurogenetics, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Werner,  Hauke B.
Neurogenetics, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Citation

Erwig, M. S., Patzig, J., Steyer, A. M., Dibaj, P., Heilmann, M., Heilmann, I., et al. (2019). Anillin facilitates septin assembly to prevent pathological outfoldings of central nervous system myelin. eLife, 8: e43888. doi:10.7554/eLife.43888.


Cite as: https://hdl.handle.net/21.11116/0000-0002-DCC1-C
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.