Broad substrate specificity ATP-binding cassette transporter ABCG2

Definition:

Broad substrate specificity ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes a wide variety of physiological compounds, dietary toxins and xenobiotics from cells. Involved in porphyrin homeostasis, mediating the export of protoporphyrin IX (PPIX) from both mitochondria to cytosol and cytosol to extracellular space, it also functions in the cellular export of heme. Also mediates the efflux of sphingosine-1-P from cells. Acts as a urate exporter functioning in both renal and extrarenal urate excretion. In kidney, it also functions as a physiological exporter of the uremic toxin indoxyl sulfate (By similarity). Also involved in the excretion of steroids like estrone 3-sulfate/E1S, 3beta-sulfooxy-androst-5-en-17-one/DHEAS, and other sulfate conjugates. Mediates the secretion of the riboflavin and biotin vitamins into milk (By similarity). Extrudes pheophorbide a, a phototoxic porphyrin catabolite of chlorophyll, reducing its bioavailability (By similarity). Plays an important role in the exclusion of xenobiotics from the brain (Probable). It confers to cells a resistance to multiple drugs and other xenobiotics including mitoxantrone, pheophorbide, camptothecin, methotrexate, azidothymidine, and the anthracyclines daunorubicin and doxorubicin, through the control of their efflux. In placenta, it limits the penetration of drugs from the maternal plasma into the fetus (By similarity). May play a role in early stem cell self-renewal by blocking differentiation (By similarity).

References:

[1]. H Komatani, et al. Identification of breast cancer resistant protein/mitoxantrone resistance/placenta-specific, ATP-binding cassette transporter as a transporter of NB-506 and J-107088, topoisomerase I inhibitors with an indolocarbazole structure. Cancer Res. 2001 Apr 1;61(7):2827-32. [Content Brief]

[2]. Nicholas M I Taylor, et al. Structure of the human multidrug transporter ABCG2. Nature. 2017 Jun 22;546(7659):504-509. [Content Brief]

[3]. Michiko Suzuki, et al. ABCG2 transports sulfated conjugates of steroids and xenobiotics. J Biol Chem. 2003 Jun 20;278(25):22644-9. [Content Brief]

[4]. Wandong Zhang, et al. The expression and functional characterization of ABCG2 in brain endothelial cells and vessels. FASEB J. 2003 Nov;17(14):2085-7. [Content Brief]

[5]. Ioannis Manolaridis, et al. Cryo-EM structures of a human ABCG2 mutant trapped in ATP-bound and substrate-bound states. Nature. 2018 Nov;563(7731):426-430. [Content Brief]

[6]. Kazuaki Takabe, et al. Estradiol induces export of sphingosine 1-phosphate from breast cancer cells via ABCC1 and ABCG2. J Biol Chem. 2010 Apr 2;285(14):10477-86. [Content Brief]

[7]. Elodie Desuzinges-Mandon, et al. ABCG2 transports and transfers heme to albumin through its large extracellular loop. J Biol Chem. 2010 Oct 22;285(43):33123-33133. [Content Brief]

[8]. Yu Toyoda, et al. Functional Characterization of Clinically-Relevant Rare Variants in ABCG2 Identified in a Gout and Hyperuricemia Cohort. Cells. 2019 Apr 18;8(4):363. [Content Brief]

[9]. Boglárka Zámbó, et al. Cellular expression and function of naturally occurring variants of the human ABCG2 multidrug transporter. Cell Mol Life Sci. 2020 Jan;77(2):365-378. [Content Brief]

[10]. Owen M Woodward, et al. Identification of a urate transporter, ABCG2, with a common functional polymorphism causing gout. Proc Natl Acad Sci U S A. 2009 Jun 23;106(25):10338-42. [Content Brief]

[11]. Hirotsugu Kobuchi, et al. Mitochondrial localization of ABC transporter ABCG2 and its function in 5-aminolevulinic acid-mediated protoporphyrin IX accumulation. PLoS One. 2012;7(11):e50082. [Content Brief]

[12]. Hirotaka Matsuo, et al. Common defects of ABCG2, a high-capacity urate exporter, cause gout: a function-based genetic analysis in a Japanese population. Sci Transl Med. 2009 Nov 4;1(5):5ra11. [Content Brief]

[13]. Akiyoshi Nakayama, et al. ABCG2 is a high-capacity urate transporter and its genetic impairment increases serum uric acid levels in humans. Nucleosides Nucleotides Nucleic Acids. 2011 Dec;30(12):1091-7. [Content Brief]

[14]. Csilla Ozvegy-Laczka, et al. Single amino acid (482) variants of the ABCG2 multidrug transporter: major differences in transport capacity and substrate recognition. Biochim Biophys Acta. 2005 Feb 1;1668(1):53-63. [Content Brief]

[15]. Yingqiu Xie, et al. The 44-kDa Pim-1 kinase phosphorylates BCRP/ABCG2 and thereby promotes its multimerization and drug-resistant activity in human prostate cancer cells. J Biol Chem. 2008 Feb 8;283(6):3349-3356. [Content Brief]

[16]. John D Allen, et al. Potent and specific inhibition of the breast cancer resistance protein multidrug transporter in vitro and in mouse intestine by a novel analogue of fumitremorgin C. Mol Cancer Ther. 2002 Apr;1(6):417-25. [Content Brief]

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