Multidrug resistance protein 1 is not associated to detergent-resistant membranes.
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.
Cerf
Emilie
E
Structure et Fonction des Membranes Biologiques, Centre de Biologie Structurale et de Bioinformatique, Université Libre de Bruxelles, Boulevard du Triomphe, B-1050 Brussels, Belgium.
Gasper
Régis
R
Belani
Jitendra D
JD
Rychnovsky
Scott
S
Chang
Xiu-Bao
XB
Buyse
Frédéric
F
Ruysschaert
Jean-Marie
JM
D020168:ATP Binding Cassette Transporter, Subfamily B, Member 1 / Q000235:genetics / Q000378:metabolism*; D000251:Adenosine Triphosphatases / Q000378:metabolism; D001692:Biological Transport; D002460:Cell Line; D002462:Cell Membrane / Q000187:drug effects* / Q000378:metabolism*; D006801:Humans; D018613:Microscopy, Confocal; D017830:Octoxynol / Q000494:pharmacology*; D011485:Protein Binding
D020168:ATP Binding Cassette Transporter, Subfamily B, Member 1; D017830:Octoxynol; D000251:Adenosine Triphosphatases