ABCMdb

ABCG2 p.Arg482Ile

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Publications

PMID: 15670731 [PubMed] Ozvegy-Laczka C et al: "Single amino acid (482) variants of the ABCG2 multidrug transporter: major differences in transport capacity and substrate recognition."

No. Sentence Comment

48 The two internal complementary primer pairs containing the specific mutation were: 5V-tta tta cca atg atc atg tta cc-3Vand 5-Vgg taa cat gat cat tgg taa taa-3V (R482I), 5V-tta tca gat cta tta ccc atg-3Vand 5V-gg taa cat cat cat ggg taa t-3V(R482M), 5V-ta ccc atg tcg atg tta cca a-3Vand 5V-t tgg taa cat cga cat ggg ta-3V(R482S), 5V-cc atg gac atg tta cca tcg att ata-3V and 5V-tat aat cga tgg taa cat gtc cat gg-3V (R482D), 5V-atg tta cca tcg att ata ttt acc-3Vand 5V-cc atg aat atg tta cca tcg att ata-3V (R482N), 5V-tta tta cct atg aag atg tta-3V cc and 5V-gg taa cat ctt cat agg taa taa-3V(R482K) and 5V-tta tta cct atg tac atg tta cc-3Vand 5V-gg taa cat gta cat agg taa taa-3V (R482Y). Login to comment
82 The expression levels of the R482I and the R482D variants were usually somewhat lower than those for the other mutants. Login to comment
117 When tested in the ATPase assay, prazosin was found to stimulate the activity of the R482I, M, S, D and N mutants by 1.3-to 1.6-fold. Login to comment
123 Panel B: Concentration dependence of MTX uptake by wtABCG2, R482I, R482K and K86M. Login to comment
124 Sf9 membrane vesicles (90 Ag) containing wtABCG2 (solid square), K86M (open square), R482I (diamond), and R482K (cross) were incubated in the presence or absence of 4 mM MgATP, with (up-triangle) or without 1 AM Ko143, with different MTX concentrations (10-3000 AM in a final volume of 150 Al) at 37 8C for 5 min. Login to comment
145 We found that none of the Arg-482 mutants had any measurable MTX uptake, as compared to the inactive ABCG2-K86M mutant (see Fig. 3B for R482I and for R482K; the data for the other variants are not shown). Login to comment
168 The R482I mutant was also active in this assay, but it had a decreased Hst-transport activity when compared to the wild-type protein, which may be due to a lower expression level of this mutant (not shown). Login to comment

PMID: 16815914 [PubMed] Ejendal KF et al: "The nature of amino acid 482 of human ABCG2 affects substrate transport and ATP hydrolysis but not substrate binding."

No. Sentence Comment

114 O¨ zvegy-Laczka et al. (2005a) selected eight of these 15 R482 variants and the R482I mutant to further study substrate transport and ATPase activity in insect cells. Login to comment

PMID: 24384916 [PubMed] Telbisz A et al: "Regulation of the function of the human ABCG2 multidrug transporter by cholesterol and bile acids: effects of mutations in potential substrate and steroid binding sites."

No. Sentence Comment

96 In contrast, in the case of the R482I, K, M, and Y variants, similarly to the wild-type ABCG2, cholesterol enrichment significantly improved the ratio of substrate stimulation, as examined after the addition of prazosin (Fig. 1A). Login to comment
109 When the cells were loaded with cholesterol, this Hst dye uptake was significantly improved in the wild-type and the R482I and M variants. Login to comment
115 Cholesterol loading significantly increased R123 extrusion in cells expressing the R482I and M variants, while there was no measurable effect in the D, G, N, S, or T variants. Login to comment
225 These were the R482G and R482S variants, which are fully active already at low membrane cholesterol levels, and the R482K and R482I mutants, which show similar cholesterol-sensing capability to the wtABCG2 (see earlier). Login to comment
252 Members of the first cluster, also including the wild-type protein (R), contain large (hydrophobic or positively charged) amino acids, represented by R482I, M, K, and Y. Login to comment