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Dev Cell. 2015 Jul 27;34(2):152-67. doi: 10.1016/j.devcel.2015.06.011. Epub 2015 Jul 9.

CNS myelin wrapping is driven by actin disassembly.

Author information

1
Department of Neurobiology, Stanford University School of Medicine, Stanford, CA 94305, USA. Electronic address: brad.zuchero@gmail.com.
2
Department of Neurobiology, Stanford University School of Medicine, Stanford, CA 94305, USA.
3
Department of Neurosurgery, Stanford University School of Medicine, Stanford, CA 94305, USA.
4
Department of Neurosciences, Case Western Reserve University School of Medicine, Cleveland, OH 44106, USA.
5
Myelin Repair Foundation, Saratoga, CA 95070, USA.
6
Klinik für Psychiatrie und Psychotherapie, Charité-Universitätsmedizin Berlin, Charité Campus Mitte, 10117 Berlin, Germany; Klinik und Poliklinik für Neurologie, Charité-Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany.
7
Klinik und Poliklinik für Neurologie, Charité-Universitätsmedizin Berlin, Charitéplatz 1, 10117 Berlin, Germany.
8
Departments of Cell Biology and Neurobiology, Duke University Medical School, Durham, NC 27710, USA.

Erratum in

  • Dev Cell. 2015 Sep 14;34(5):608. Leonoudakus, Dmitri [corrected to Leonoudakis, Dmitri].

Abstract

Myelin is essential in vertebrates for the rapid propagation of action potentials, but the molecular mechanisms driving its formation remain largely unknown. Here we show that the initial stage of process extension and axon ensheathment by oligodendrocytes requires dynamic actin filament assembly by the Arp2/3 complex. Unexpectedly, subsequent myelin wrapping coincides with the upregulation of actin disassembly proteins and rapid disassembly of the oligodendrocyte actin cytoskeleton and does not require Arp2/3. Inducing loss of actin filaments drives oligodendrocyte membrane spreading and myelin wrapping in vivo, and the actin disassembly factor gelsolin is required for normal wrapping. We show that myelin basic protein, a protein essential for CNS myelin wrapping whose role has been unclear, is required for actin disassembly, and its loss phenocopies loss of actin disassembly proteins. Together, these findings provide insight into the molecular mechanism of myelin wrapping and identify it as an actin-independent form of mammalian cell motility.

PMID:
26166300
PMCID:
PMC4519368
DOI:
10.1016/j.devcel.2015.06.011
[Indexed for MEDLINE]
Free PMC Article

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