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dc.contributor.authorRaasakka, Arneen_US
dc.contributor.authorJones, Nykola Cen_US
dc.contributor.authorHoffmann, Søren Ven_US
dc.contributor.authorKursula, Petrien_US
dc.PublishedRaasakka A, Jones, Hoffmann SV, Kursula P. Ionic strength and calcium regulate membrane interactions of myelin basic protein and the cytoplasmic domain of myelin protein zero. Biochemical and Biophysical Research Communications - BBRC. 2019;511(1):7-12eng
dc.description.abstractThe formation of a mature myelin sheath in the vertebrate nervous system requires specific protein-membrane interactions. Several myelin-specific proteins are involved in stacking lipid membranes into multilayered structures around axons, and misregulation of these processes may contribute to chronic demyelinating diseases. Two key proteins in myelin membrane binding and stacking are the myelin basic protein (MBP) and protein zero (P0). Other factors, including Ca2+, are important for the regulation of myelination. We studied the effects of ionic strength and Ca2+ on the membrane interactions of MBP and the cytoplasmic domain of P0 (P0ct). MBP and P0ct bound and aggregated negatively charged lipid vesicles, while simultaneously folding, and both ionic strength and calcium had systematic effects on these interactions. When decreasing membrane net negative charge, the level and kinetics of vesicle aggregation were affected by both salt and Ca2+. The effects on lipid membrane surfaces by ions can directly affect myelin protein-membrane interactions, in addition to signalling effects in myelinating glia.en_US
dc.rightsAttribution CC BYeng
dc.titleIonic strength and calcium regulate membrane interactions of myelin basic protein and the cytoplasmic domain of myelin protein zeroen_US
dc.typePeer reviewed
dc.typeJournal article
dc.rights.holderCopyright 2019 The Author(s)
dc.source.journalBiochemical and Biophysical Research Communications - BBRC
dc.relation.projectNorges forskningsråd: 247669

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