Multidrug resistance protein 1 is not associated to detergent-resistant membranes

Emilie Cerf, Régis Gasper, Scott Rychnovsky, Xiu bao Chang, Frédéric Buyse, Jean Marie Ruysschaert

Research output: Contribution to journalArticle

10 Scopus citations

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 C4, 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.

Original languageEnglish (US)
Pages (from-to)1025-1030
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume355
Issue number4
DOIs
StatePublished - Apr 20 2007

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Keywords

  • ATP-binding cassette (ABC)
  • ATPase activity
  • Cholesterol
  • Detergent-resistant membrane
  • MRP1
  • Transport activity

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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