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Bakhti, M. ; Aggarwal, S.* ; Simons, M.*

Myelin architecture: Zippering membranes tightly together.

Cell. Mol. Life Sci. 71, 1265-1277 (2014)
DOI Verlagsversion bestellen
Open Access Green möglich sobald Postprint bei der ZB eingereicht worden ist.
Rapid nerve conduction requires the coating of axons by a tightly packed multilayered myelin membrane. In the central nervous system, myelin is formed from cellular processes that extend from oligodendrocytes and wrap in a spiral fashion around an axon, resulting in the close apposition of adjacent myelin membrane bilayers. In this review, we discuss the physical principles underlying the zippering of the plasma membrane of oligodendrocytes at the cytoplasmic and extracellular leaflet. We propose that the interaction of the myelin basic protein with the cytoplasmic leaflet of the myelin bilayer triggers its polymerization into a fibrous network that drives membrane zippering and protein extrusion. In contrast, the adhesion of the extracellular surfaces of myelin requires the down-regulation of repulsive components of the glycocalyx, in order to uncover weak and unspecific attractive forces that bring the extracellular surfaces into close contact. Unveiling the mechanisms of myelin membrane assembly at the cytoplasmic and extracelluar sites may help to understand how the myelin bilayers are disrupted and destabilized in the different demyelinating diseases.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Review
Schlagwörter Myelin; Oligodendrocytes; Myelin basic protein; Proteolipid protein; Central-nervous-system; Intrinsically Unstructured Proteins; Acidic Lipid Vesicles; Basic-protein; Cell-adhesion; Multiple-sclerosis; Cns Myelin; Proteolipid Protein; Posttranslational Modifications; Peptidylarginine Deiminase
ISSN (print) / ISBN 1420-682X
e-ISSN 1420-9071
Quellenangaben Band: 71, Heft: 7, Seiten: 1265-1277 Artikelnummer: , Supplement: ,
Verlag Birkhäuser
Verlagsort Basel
Begutachtungsstatus Peer reviewed