Journal
CELL REPORTS
Volume 18, Issue 2, Pages 314-323Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2016.12.053
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Funding
- ERC CoG grant [647168]
- German Research Foundation [SI 746/9-1, SI 746/10-1, SPP1757, TRR128, TRR43]
- Tschira-Stiftung
- ERC advanced grant Ax-oGLIA
- ERC advanced grant MyeliNANO
- Cluster of Excellence
- SyNergy
- Academy of Finland [252066]
- Emil Aaltonen Foundation
- Sigrid Juselius Foundation
- DFG
- Academy of Finland (AKA) [252066, 252066] Funding Source: Academy of Finland (AKA)
- European Research Council (ERC) [647168] Funding Source: European Research Council (ERC)
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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,'3'-cyclic nucleotide 3'-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.
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