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Elife. 2019 Jan 23;8. pii: e43888. doi: 10.7554/eLife.43888.

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

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Department of Neurogenetics, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
Electron Microscopy Core Unit, Max Planck Institute of Experimental Medicine, Göttingen, Germany.
Center for Nanoscale Microscopy and Molecular Physiology of the Brain, Göttingen, Germany.
Department of Cellular Biochemistry, Institute of Biochemistry and Biotechnology, Martin-Luther-University Halle-Wittenberg, Halle, Germany.
Proteomics Group, Max Planck Institute of Experimental Medicine, Göttingen, Germany.


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.


anillin (ANLN); focused ion beam scanning electron microscopy (FIB-SEM); mouse; myelin outfoldings / redundant myelin; myelin pathology; neuroscience; oligodendrocyte; septin filament

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