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Søren Vrønning Hoffmann

Ionic strength and calcium regulate membrane interactions of myelin basic protein and the cytoplasmic domain of myelin protein zero

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The 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 Ca 2+ , are important for the regulation of myelination. We studied the effects of ionic strength and Ca 2+ 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 Ca 2+ . The effects on lipid membrane surfaces by ions can directly affect myelin protein-membrane interactions, in addition to signalling effects in myelinating glia.

Original languageEnglish
JournalBiochemical and Biophysical Research Communications
Volume511
Issue1
Pages (from-to)7-12
Number of pages6
ISSN0006-291X
DOIs
Publication statusPublished - 2019

    Research areas

  • Calcium, Intrinsic disorder, Lipid binding, Myelin basic protein, Protein folding, Protein zero, CELLS, ZINC-BINDING

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