Journal
DEVELOPMENTAL CELL
Volume 34, Issue 2, Pages 152-167Publisher
CELL PRESS
DOI: 10.1016/j.devcel.2015.06.011
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Funding
- NIH [NS069375, 1S10RR02678001, R01 EY10257, R01 MH103374, T32 HD007249, F30 MH106261]
- National Multiple Sclerosis Society (NMSS)
- Myelin Repair Foundation
- Sheldon and Miriam Adelson Medical Foundation
- Deutsche Forschungsgemeinschaft
- BMBF (Center for Stroke Research Berlin)
- NMSS Career Transition Award
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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.
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