Functional Role of Arginine 375 in Transmembrane Helix 6 of Multidrug Resistance Protein 4 (MRP4/ABCC4)

  title={Functional Role of Arginine 375 in Transmembrane Helix 6 of Multidrug Resistance Protein 4 (MRP4/ABCC4)},
  author={A. A. El-Sheikh and J. J. van den Heuvel and E. Krieger and F. Russel and J. Koenderink},
  journal={Molecular Pharmacology},
  pages={964 - 971}
  • A. A. El-Sheikh, J. J. van den Heuvel, +2 authors J. Koenderink
  • Published 2008
  • Biology, Medicine
  • Molecular Pharmacology
  • Multidrug resistance protein (MRP) 4 transports a variety of endogenous and xenobiotic organic anions. MRP4 is widely expressed in the body and specifically localized to the renal apical proximal tubule cell membrane, where it mediates the excretion of these compounds into urine. To characterize the MRP4 substrate-binding site, the amino acids Phe368, Phe369, Glu374, Arg375, and Glu378 of transmembrane helix 6, and Arg998 of helix 12, localized in the intracellular half of the central pore… CONTINUE READING
    42 Citations
    The Pharmacological and Physiological Role of Multidrug-Resistant Protein 4
    • 37
    • PDF
    Polymorphic variants of MRP4/ABCC4 differentially modulate the transport of methylated arsenic metabolites and physiological organic anions.
    • 24
    • Highly Influenced
    Identification and Functional Characterization of a GSH Conjugate Efflux Pathway in the Rat Lens.
    • 4
    • PDF
    Multidrug Resistance Protein 1 (MRP1, ABCC1), a “Multitasking” ATP-binding Cassette (ABC) Transporter*
    • S. Cole
    • Biology, Medicine
    • The Journal of Biological Chemistry
    • 2014
    • 158
    • PDF
    MRP4 is responsible for the efflux transport of mycophenolic acid β-d glucuronide (MPAG) from hepatocytes to blood


    Functional Importance of Polar and Charged Amino Acid Residues in Transmembrane Helix 14 of Multidrug Resistance Protein 1 (MRP1/ABCC1)
    • 43
    • PDF
    Identification of Basic Residues Involved in Drug Export Function of Human Multidrug Resistance-associated Protein 2*
    • 83
    • PDF
    Identification of a Nonconserved Amino Acid Residue in Multidrug Resistance Protein 1 Important for Determining Substrate Specificity
    • 65
    • PDF
    Mutation of a Single Conserved Tryptophan in Multidrug Resistance Protein 1 (MRP1/ABCC1) Results in Loss of Drug Resistance and Selective Loss of Organic Anion Transport*
    • 142
    • Highly Influential
    • PDF
    Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins.
    • 674
    • PDF