Affiliations: University Joseph Fourier, Grenoble, France | Institut Laue-Langevin, Grenoble, France | CNR-IOM, OGG, c/o Institut Laue-Langevin, Grenoble, France | Institut de Biologie Structurale, Grenoble, France | Department of Biochemistry, University of Oulu, Oulu, Finland
Note: [] Corresponding author: Dr. F. Natali, CNR-IOM, c/o Institut Laue-Langevin, BP 1566, rue Jules Horowitz, 38042 Grenoble Cedex 9, France. Tel.: +33 4 76 20 70 71; Fax: +33 4 76 20 76 88; E-mail: [email protected].
Abstract: Myelin is a multilamellar membrane which, wrapping the nerve axons, increases the efficiency of nervous signal transmission. Indeed, the molecular components of the myelin sheath interact tightly with each other and molecules on the axonal surface to drive myelination, to keep both myelin and the axon intact, and to transduce signals from myelin to the axon and vice versa. Myelin is strongly affected in human demyelinating diseases in both the central and peripheral nervous system (CNS and PNS, respectively). Despite the presence of a well-defined set of myelin-specific proteins, little is known about the structure and the dynamics of these proteins, their interactions with the membrane and their influence on myelin stability. We present here the first neutron scattering results on the dynamics of the myelin sheath in PNS and of the interaction between its constituents. Specifically, the human P2 protein is shown to stabilize the lipid membrane upon binding to it.
