Echinophilic proteins stomatin, sorcin, and synexin locate outside gangliosideM1 (GM1) patches in the erythrocyte membrane |
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Authors: | Lucyna Mró wczyńska,Ulrich Salzer,Ale&scaron Igli? |
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Affiliation: | a Department of Cell Biology, A. Mickiewicz University, PL-61614, Poznań, Poland b Max F. Perutz Laboratories, Medical University of Vienna, A-1030 Vienna, Austria c Laboratory of Biophysics, Faculty of Electrical Engineering, University of Ljubljana, SI-1000 Ljubljana, Slovenia d Department of Biology, Åbo Akademi University, FIN-20520 Åbo-Turku, Finland |
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Abstract: | The detergent (Triton X-100, 4 °C)-resistant membrane (DRM)-associated membrane proteins stomatin, sorcin, and synexin (anexin VII) exposed on the cytoplasmic side of membrane were investigated for their lateral distribution in relation to induced gangliosideM1 (GM1) raft patches in flat (discocytic) and curved (echinocytic) human erythrocyte membrane. In discocytes, no accumulation of stomatin, sorcin, and synexin in cholera toxin subunit B (CTB) plus anti-CTB-induced GM1 patches was detected by fluorescence microscopy. In echinocytes, stomatin, sorcin, and synexin showed a similar curvature-dependent lateral distribution as GM1 patches by accumulating to spiculae induced by ionophore A23187 plus calcium. Stomatin was partly and synexin and sorcin were fully recruited to the spiculae. However, the DRM-associated proteins only partially co-localized with GM1 and were frequently distributed into different spiculae than GM1. The study indicates that stomatin, sorcin, and synexin are echinophilic membrane components that mainly locate outside GM1 rafts in the human erythrocyte membrane. Echinophilicity is suggested to contribute to the DRM association of a membrane component in general. |
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Keywords: | Ganglioside GM1 Membrane curvature Erythrocyte DRM Fluorescence microscopy |
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