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  Reorganization of lipid diffusion by myelin basic protein as revealed by STED nanoscopy.

Steshenko, S. O., Andrade, D., Honigmann, A., Müller, V., Schneider, D., Sezgin, E., et al. (2016). Reorganization of lipid diffusion by myelin basic protein as revealed by STED nanoscopy. Biophysical Journal, 110(11), 2441-2450. doi:10.1016/j.bpj.2016.04.047.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-DA62-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-2030-8
Genre: Journal Article

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Steshenko, S. O., Author
Andrade, D.1, Author              
Honigmann, A.1, Author              
Müller, V.1, Author              
Schneider, D., Author
Sezgin, E., Author
Hell, S. W.1, Author              
Simons, M., Author
Eggeling, C.1, Author              
Affiliations:
1Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society, ou_578627              

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 Abstract: Myelin is a multilayered membrane that ensheathes axonal fibers in the vertebrate nervous system, allowing fast propagation of nerve action potentials. It contains densely packed lipids, lacks an actin-based cytocortex, and requires myelin basic protein (MBP) as its major structural component. This protein is the basic constituent of the proteinaceous meshwork that is localized between adjacent cytoplasmic membranes of the myelin sheath. Yet, it is not clear how MBP influences the organization and dynamics of the lipid constituents of myelin. Here, we used optical stimulated emission depletion super-resolution microscopy in combination with fluorescence correlation spectroscopy to assess the characteristics of diffusion of different fluorescent lipid analogs in myelin membrane sheets of cultured oligodendrocytes and in micrometer-sized domains that were induced by MBP in live epithelial PtK2 cells. Lipid diffusion was significantly faster and less anomalous both in oligodendrocytes and inside the MBP-rich domains of PtK2 cells compared with undisturbed live PtK2 cells. Our data show that MBP reorganizes lipid diffusion, possibly by preventing the buildup of an actin-based cytocortex and by preventing most membrane proteins from entering the myelin sheath region. Yet, in contrast to myelin sheets in oligodendrocytes, the MBP-induced domains in epithelial PtK2 cells demonstrate no change in lipid order, indicating that segregation of long-chain lipids into myelin sheets is a process specific to oligodendrocytes.

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Language(s): eng - English
 Dates: 2016-06-072016-06-07
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1016/j.bpj.2016.04.047
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Title: Biophysical Journal
Source Genre: Journal
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Pages: - Volume / Issue: 110 (11) Sequence Number: - Start / End Page: 2441 - 2450 Identifier: -