Antagonistic functions of MBP and CNP establish cytosolic channels in CNS myelin
Snaidero, Nicolas; Velte, Caroline; Myllykoski, Matti; Raasakka, Arne; Ignatev, Alexander; Werner, Hauke B.; Erwig, Michelle S.; Möbius, Wiebke; Kursula, Petri; Nave, Klaus-Armin; Simons, Mikael (2017-01-10)
Nicolas Snaidero, Caroline Velte, Matti Myllykoski, Arne Raasakka, Alexander Ignatev, Hauke B. Werner, Michelle S. Erwig, Wiebke Möbius, Petri Kursula, Klaus-Armin Nave, Mikael Simons, Antagonistic Functions of MBP and CNP Establish Cytosolic Channels in CNS Myelin, Cell Reports, Volume 18, Issue 2, 10 January 2017, Pages 314-323, ISSN 2211-1247, http://dx.doi.org/10.1016/j.celrep.2016.12.053. (http://www.sciencedirect.com/science/article/pii/S2211124716317600)
© 2016 The Author(s). Under a Creative Commons license https://creativecommons.org/licenses/by-nc-nd/4.0/
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 a molecular and structural framework for understanding how myelin maintains its cytoplasm to function as an active axon-glial unit.
- Avoin saatavuus