Functional Role of Arginine 375 in Transmembrane Helix 6 of Multidrug Resistance Protein 4 (MRP4/ABCC4)
@article{ElSheikh2008FunctionalRO, 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}, year={2008}, volume={74}, pages={964 - 971} }
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
Figures, Tables, and Topics from this paper
42 Citations
Phenylalanine 368 of multidrug resistance-associated protein 4 (MRP4/ABCC4) plays a crucial role in substrate-specific transport activity.
- Chemistry, Medicine
- Biochemical pharmacology
- 2012
- 21
The Pharmacological and Physiological Role of Multidrug-Resistant Protein 4
- Biology, Medicine
- The Journal of Pharmacology and Experimental Therapeutics
- 2015
- 37
- PDF
Structural patterns of the human ABCC4/MRP4 exporter in lipid bilayers rationalize clinically observed polymorphisms
- Chemistry, Medicine
- Pharmacological research
- 2018
- 9
Polymorphic variants of MRP4/ABCC4 differentially modulate the transport of methylated arsenic metabolites and physiological organic anions.
- Chemistry, Medicine
- Biochemical pharmacology
- 2016
- 24
- Highly Influenced
Identification and Functional Characterization of a GSH Conjugate Efflux Pathway in the Rat Lens.
- Biology, Medicine
- Investigative ophthalmology & visual science
- 2015
- 4
- PDF
Multidrug Resistance Protein 1 (MRP1, ABCC1), a “Multitasking” ATP-binding Cassette (ABC) Transporter*
- 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
- Chemistry, Medicine
- Xenobiotica; the fate of foreign compounds in biological systems
- 2020
Localization of putative binding sites for cyclic guanosine monophosphate and the anti-cancer drug 5-fluoro-2′-deoxyuridine-5′-monophosphate on ABCC11 in silico models
- Biology, Medicine
- BMC Structural Biology
- 2012
- 7
References
SHOWING 1-10 OF 50 REFERENCES
Functional Importance of Polar and Charged Amino Acid Residues in Transmembrane Helix 14 of Multidrug Resistance Protein 1 (MRP1/ABCC1)
- Biology, Medicine
- Journal of Biological Chemistry
- 2003
- 43
- PDF
Mutation of Trp1254 in the multispecific organic anion transporter, multidrug resistance protein 2 (MRP2) (ABCC2), alters substrate specificity and results in loss of methotrexate transport activity.
- Biology, Medicine
- The Journal of biological chemistry
- 2001
- 119
- Highly Influential
Identification of Basic Residues Involved in Drug Export Function of Human Multidrug Resistance-associated Protein 2*
- Medicine, Biology
- The Journal of Biological Chemistry
- 2000
- 83
- PDF
Identification of a Nonconserved Amino Acid Residue in Multidrug Resistance Protein 1 Important for Determining Substrate Specificity
- Biology, Medicine
- The Journal of Biological Chemistry
- 2001
- 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*
- Medicine, Biology
- The Journal of Biological Chemistry
- 2001
- 142
- Highly Influential
- PDF
Identification of Proline Residues in the Core Cytoplasmic and Transmembrane Regions of Multidrug Resistance Protein 1 (MRP1/ABCC1) Important for Transport Function, Substrate Specificity, and Nucleotide Interactions*
- Biology, Medicine
- Journal of Biological Chemistry
- 2004
- 64
- PDF
A positively charged amino acid proximal to the C-terminus of TM17 of MRP1 is indispensable for GSH-dependent binding of substrates and for transport of LTC4.
- Biology, Medicine
- Biochemistry
- 2002
- 32
Transmembrane helix 11 of multidrug resistance protein 1 (MRP1/ABCC1): identification of polar amino acids important for substrate specificity and binding of ATP at nucleotide binding domain 1.
- Biology, Medicine
- Biochemistry
- 2004
- 27
- Highly Influential
Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins.
- Biology, Medicine
- Physiological reviews
- 2006
- 674
- PDF