Vis enkel innførsel

dc.contributor.authorRaasakka, Arneen_US
dc.contributor.authorRuskamo, Sallaen_US
dc.contributor.authorKowal, Juliaen_US
dc.contributor.authorHan, Huijongen_US
dc.contributor.authorBaumann, Anneen_US
dc.contributor.authorMyllykoski, Mattien_US
dc.contributor.authorFasano, Annaen_US
dc.contributor.authorRossano, Roccoen_US
dc.contributor.authorRiccio, Paoloen_US
dc.contributor.authorBürck, Jochenen_US
dc.contributor.authorUlrich, Anne S.en_US
dc.contributor.authorStahlberg, Henningen_US
dc.contributor.authorKursula, Petrien_US
dc.PublishedRaasakka A, Ruskamo S, Kowal J, Han H, Baumann A, Myllykoski M, Fasano, Rossano, Riccio, Bürck J, Ulrich AS, Stahlberg H, Kursula P. Molecular structure and function of myelin protein P0 in membrane stacking. Scientific Reports. 2019;9:642eng
dc.description.abstractCompact myelin forms the basis of nerve insulation essential for higher vertebrates. Dozens of myelin membrane bilayers undergo tight stacking, and in the peripheral nervous system, this is partially enabled by myelin protein zero (P0). Consisting of an immunoglobulin (Ig)-like extracellular domain, a single transmembrane helix, and a cytoplasmic extension (P0ct), P0 harbours an important task in ensuring the integrity of compact myelin in the extracellular compartment, referred to as the intraperiod line. Several disease mutations resulting in peripheral neuropathies have been identifed for P0, refecting its physiological importance, but the arrangement of P0 within the myelin ultrastructure remains obscure. We performed a biophysical characterization of recombinant P0ct. P0ct contributes to the binding afnity between apposed cytoplasmic myelin membrane leafets, which not only results in changes of the bilayer properties, but also potentially involves the arrangement of the Iglike domains in a manner that stabilizes the intraperiod line. Transmission electron cryomicroscopy of native full-length P0 showed that P0 stacks lipid membranes by forming antiparallel dimers between the extracellular Ig-like domains. The zipper-like arrangement of the P0 extracellular domains between two membranes explains the double structure of the myelin intraperiod line. Our results contribute to the understanding of PNS myelin, the role of P0 therein, and the underlying molecular foundation of compact myelin stability in health and disease.en_US
dc.publisherNature Researcheng
dc.relation.ispartof<a href="" target="blank"> The Characterization of Disordered Membrane-Binding Proteins of Myelin. A Biophysical Approach</a>
dc.rightsAttribution CC BYeng
dc.titleMolecular structure and function of myelin protein P0 in membrane stackingen_US
dc.typePeer reviewed
dc.typeJournal article
dc.rights.holderCopyright the Author(s) 2019

Tilhørende fil(er)


Denne innførselen finnes i følgende samling(er)

Vis enkel innførsel

Attribution CC BY
Med mindre annet er angitt, så er denne innførselen lisensiert som Attribution CC BY