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  Scanning STED-FCS reveals spatiotemporal heterogeneity of lipid interaction in the plasma membrane of living cells.

Honigmann, A., Müller, V., Ta, H., Schönle, A., Sezgin, E., Hell, S. W., et al. (2014). Scanning STED-FCS reveals spatiotemporal heterogeneity of lipid interaction in the plasma membrane of living cells. Nature Communications, 5: 5412. doi:10.1038/ncomms6412.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-435B-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CC88-5
Genre: Journal Article

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 Creators:
Honigmann, A.1, Author              
Müller, V.1, Author              
Ta, H.1, Author              
Schönle, A.1, Author              
Sezgin, E., Author
Hell, S. W.1, Author              
Eggeling, C.1, Author              
Affiliations:
1Department of NanoBiophotonics, MPI for biophysical chemistry, Max Planck Society, ou_578627              

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 Abstract: The interaction of lipids and proteins plays an important role in plasma membrane bioactivity, and much can be learned from their diffusion characteristics. Here we present the combination of super-resolution STED microscopy with scanning fluorescence correlation spectroscopy (scanning STED-FCS, sSTED-FCS) to characterize the spatial and temporal heterogeneity of lipid interactions. sSTED-FCS reveals transient molecular interaction hotspots for a fluorescent sphingolipid analogue. The interaction sites are smaller than 80nm in diameter and lipids are transiently trapped for several milliseconds in these areas. In comparison, newly developed fluorescent phospholipid and cholesterol analogues with improved phase-partitioning properties show more homogenous diffusion, independent of the preference for liquid-ordered or disordered membrane environments. Our results do not support the presence of nanodomains based on lipid-phase separation in the basal membrane of our cultured nonstimulated cells, and show that alternative interactions are responsible for the strong local trapping of our sphingolipid analogue.

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Language(s): eng - English
 Dates: 2014-11-20
 Publication Status: Published online
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 Rev. Method: Peer
 Identifiers: DOI: 10.1038/ncomms6412
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Title: Nature Communications
Source Genre: Journal
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Pages: 12 Volume / Issue: 5 Sequence Number: 5412 Start / End Page: - Identifier: -