Sphingolipid–Cholesterol Rafts Diffuse as Small Entities in the Plasma Membrane of Mammalian Cells
By Arnd Pralle, P. Keller, E. Florin, K. Simons, J. Hörber. Journal of Cell Biology, 2000
1,015 citations recorded by the source corpus.
To probe the dynamics and size of lipid rafts in the membrane of living cells, the local diffusion of single membrane proteins was measured. A laser trap was used to confine the motion of a bead bound to a raft protein to a small area (diam ≤ 100 nm) and to measure its local diffusion by high resolution single particle tracking. Using protein constructs with identical ectodomains and different membrane regions and vice versa, we demonstrate that this method provides the viscous damping of the membrane domain in the lipid bilayer. When glycosylphosphatidylinositol (GPI) -anchored and transmembrane proteins are raft-associated, their diffusion becomes independent of the type of membrane anchor and is significantly reduced compared with that of nonraft transmembrane proteins. Cholesterol depletion accelerates the diffusion of raft-associated proteins for transmembrane raft proteins to the level of transmembrane nonraft proteins and for GPI-anchored proteins even further. Raft-associated GPI-anchored proteins were never observed to dissociate from the raft within the measurement intervals of up to 10 min. The measurements agree with lipid rafts being cholesterol-stabilized complexes of 26 ± 13 nm in size diffusing as one entity for minutes.
Subfields: Cell Biology, Molecular Biology, Physiology
View Paper: https://www.semanticscholar.org/paper/58a7091e81bf908376b3be48aa9d722ebd808326
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Citations in the corpus
- Revitalizing membrane rafts: new tools and insights (2010, background): “This is reminiscent of live-cell analysis by photonic force microscopy, which concluded that GPI-anchored protein domains have a cholesterol-dependent size of 50 n”
- Mediators of innate immune recognition of bacteria concentrate in lipid rafts and facilitate lipopolysaccharide-induced cell activation. (2002, background): “One of the most widely appreciated roles of lipid rafts (or microdomains) is in the recruitment and concentration of molecules involved in cellular signalling (Pralle et al., 2000).”
- Biological and synthetic membranes: What can be learned from a coarse-grained description? (2006, background): “, the main chain transition in lipid bilayers from a fluid, liquid crystalline to a gel phase [18,19], and the lateral phase separation which appears to be implicated in “raft” formation in the plasma membrane [20–23], as well as thermally activated processes such as vesicle fusion and fission [24–3”
- GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated, clathrin-independent pinocytic pathway. (2002, background): “…(pH 4.6) buffers, nor released into a soluble pool in the lumensubmicron-sized domains at the cell surface (Friedrichof endosomes (data not shown), confirming the use of Fl-anti-GFPson and Kurzchalia, 1998; Pralle et al., 2000; Varma and as a marker for following endocytosis of GFP-tagged proteins.”
- Lipid rafts Published, JLR Papers in Press, February 1, 2003. DOI 10.1194/jlr.R200021-JLR200 (2003, neutral): “Single particle tracking of GPI-anchored proteins yielded a size of 26 nm (25).”
- The human ATP-binding cassette (ABC) transporter superfamily. (2001, neutral): “3,500 SM molecules (59), may vary as a consequence of cell lipid concentration and external conditions; their modifications may eventually lead to raft coalescence and dispersion of the liquid-disordered phase, with conse-”
- Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts (2003, background): “Rafts are small and highly dispersed at the cell surface and are suggested to contain only a subset of 10– 30 protein molecules (Pralle et al., 2000).”