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  Myelin membrane assembly is driven by a phase transition of myelin basic proteinsiInto a cohesive protein meshwork.

Aggarwal, S., Snaidero, N., Pähler, G., Frey, S., Sanchez, P., Zweckstetter, M., et al. (2013). Myelin membrane assembly is driven by a phase transition of myelin basic proteinsiInto a cohesive protein meshwork. PLoS Biology, 11(6): e1001577. doi:10.1371/journal.pbio.1001577.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-3A79-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-C76F-5
Genre: Journal Article

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 Creators:
Aggarwal, S., Author
Snaidero, N., Author
Pähler, G., Author
Frey, S.1, Author              
Sanchez, P., Author
Zweckstetter, M.2, Author              
Janshoff, A., Author
Schneider, A., Author
Weil, M. T., Author
Schaap, I. A. T., Author
Görlich, D.1, Author              
Simons, M., Author
Affiliations:
1Department of Cellular Logistics, MPI for biophysical chemistry, Max Planck Society, ou_578574              
2Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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 Abstract: Rapid conduction of nerve impulses requires coating of axons by myelin. To function as an electrical insulator, myelin is generated as a tightly packed, lipid-rich multilayered membrane sheath. Knowledge about the mechanisms that govern myelin membrane biogenesis is required to understand myelin disassembly as it occurs in diseases such as multiple sclerosis. Here, we show that myelin basic protein drives myelin biogenesis using weak forces arising from its inherent capacity to phase separate. The association of myelin basic protein molecules to the inner leaflet of the membrane bilayer induces a phase transition into a cohesive mesh-like protein network. The formation of this protein network shares features with amyloid fibril formation. The process is driven by phenylalanine-mediated hydrophobic and amyloid-like interactions that provide the molecular basis for protein extrusion and myelin membrane zippering. These findings uncover a physicochemical mechanism of how a cytosolic protein regulates the morphology of a complex membrane architecture. These results provide a key mechanism in myelin membrane biogenesis with implications for disabling demyelinating diseases of the central nervous system.

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Language(s): eng - English
 Dates: 2013-06-04
 Publication Status: Published online
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1371/journal.pbio.1001577
 Degree: -

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Title: PLoS Biology
Source Genre: Journal
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Pages: - Volume / Issue: 11 (6) Sequence Number: e1001577 Start / End Page: - Identifier: -