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Published on December 23, 2004; 10.1104/pp.104.053041

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Received September 6, 2004
Returned for revision October 17, 2004
Accepted October 23, 2004

Analysis of Detergent-Resistant Membranes in Arabidopsis. Evidence for Plasma Membrane Lipid Rafts

Georg H.H. Borner , D. Janine Sherrier , Thilo Weimar , Louise V. Michaelson , Nathan D. Hawkins , Andrew MacAskill , Johnathan A. Napier , Michael H. Beale , Kathryn S. Lilley , and Paul Dupree *

Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom
Crop Performance and Improvement, Rothamsted Research, Harpenden, Hertfordshire AL5 2JQ, United Kingdom
Cambridge Centre for Proteomics, University of Cambridge, Cambridge CB2 1QW, United Kingdom
Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom; Cambridge Centre for Proteomics, University of Cambridge, Cambridge CB2 1QW, United Kingdom

* Corresponding author; email: p.dupree{at}bioc.cam.ac.uk.

The trafficking and function of cell surface proteins in eukaryotic cells may require association with detergent-resistant sphingolipid- and sterol-rich membrane domains. The aim of this work was to obtain evidence for lipid domain phenomena in plant membranes. A protocol to prepare Triton X-100 detergent-resistant membranes (DRMs) was developed using Arabidopsis (Arabidopsis thaliana) callus membranes. A comparative proteomics approach using two-dimensional difference gel electrophoresis and liquid chromatography-tandem mass spectrometry revealed that the DRMs were highly enriched in specific proteins. They included eight glycosylphosphatidylinositol-anchored proteins, several plasma membrane (PM) ATPases, multidrug resistance proteins, and proteins of the stomatin/prohibitin/hypersensitive response family, suggesting that the DRMs originated from PM domains. We also identified a plant homolog of flotillin, a major mammalian DRM protein, suggesting a conserved role for this protein in lipid domain phenomena in eukaryotic cells. Lipid analysis by gas chromatography-mass spectrometry showed that the DRMs had a 4-fold higher sterol-to-protein content than the average for Arabidopsis membranes. The DRMs were also 5-fold increased in sphingolipid-to-protein ratio. Our results indicate that the preparation of DRMs can yield a very specific set of membrane proteins and suggest that the PM contains phytosterol and sphingolipid-rich lipid domains with a specialized protein composition. Our results also suggest a conserved role of lipid modification in targeting proteins to both the intracellular and extracellular leaflet of these domains. The proteins associated with these domains provide important new experimental avenues into understanding plant cell polarity and cell surface processes.




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