Multidrug resistance protein 1 is not associated to detergent-resistant membranes |
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Authors: | Cerf Emilie Gasper Régis Belani Jitendra D Rychnovsky Scott Chang Xiu-Bao Buyse Frédéric Ruysschaert Jean-Marie |
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Affiliation: | Structure et Fonction des Membranes Biologiques, Centre de Biologie Structurale et de Bioinformatique, Université Libre de Bruxelles, Boulevard du Triomphe, B-1050 Brussels, Belgium. |
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Abstract: | Multidrug resistance protein 1 (MRP1) is a member of the ATP-binding cassette superfamily. Using the energy provided by ATP hydrolysis, it transports a broad spectrum of substrates across the plasma membrane, including hormones, leukotriene C(4), bile salts, and anti-cancer drugs. Recent works have suggested that P-glycoprotein is associated to cholesterol and sphingolipid-rich membrane microdomains and that cholesterol upregulates its ATPase and drug transport activities. Confocal microscopy experiments and Triton X-100 extraction of detergent-resistant membranes provide evidence that MRP1 is not located in raft-like structures and that its activity is downregulated by cholesterol. The data are discussed in terms of cholesterol-protein interaction and topology. |
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Keywords: | ABC, ATP-binding cassette AMP, adenosine monophosphate ATP, adenosine triphosphate CFTR, cystic fibrosis transmembrane conductance regulator CRAC, cholesterol recognition/interaction amino acid consensus DRM, detergent-resistant membrane HEK, human embryonic kidney LTC4, leukotriene C4 MβCD, methyl-β-cyclodextrin MDR, multidrug resistance MRP, Multidrug resistance protein NBD, nucleotide-binding domain Pgp, P-glycoprotein SSD, sterol sensing domain TMD, transmembrane domain |
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