ABCMdb

ABCC1 p.Tyr1236Phe

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Publications

PMID: 11925441 [PubMed] Zhang DW et al: "Determinants of the substrate specificity of multidrug resistance protein 1: role of amino acid residues with hydrogen bonding potential in predicted transmembrane helix 17."

No. Sentence Comment

2 To determine whether other residues with hydrogen bonding potential within TM17 influence substrate specificity, we replaced Ser1233 , Ser1235 , Ser1237 , Gln1239 , Thr1241 , and Asn1245 with Ala and Tyr1236 and Tyr1243 with Phe. Login to comment
4 In contrast, mutations Y1236F and T1241A decreased resistance to vincristine but not to VP-16, doxorubicin, and epirubicin. Login to comment
113 Mutation of one polar-aromatic residue, Y1243F, caused an approximately 2-3-fold reduction of resistance to all four drugs, whereas three mutations, Y1236F, T1241A, and N1245A, resulted in a 2-3-fold loss of resistance to only certain drugs. Login to comment
114 Interestingly, both mutation Y1236F and mutation T1241A decreased vincristine resistance ϳ3-fold without a significant effect on the resistance to VP-16, doxorubicin, and epirubicin. Login to comment
117 Subcellular Localization of Mutant and Wild Type MRP1 in Transfected HEK293 Cells-To determine whether effects of mutations Y1236F, T1241A, Y1243F, and N1245A on the drug FIG. 1. Login to comment
141 ATP-dependent transport of [3 H]E217betaG was also examined (Fig. 5), but none of the mutations S1233A, S1235A, Y1236F, S1237A, Q1239A, and T1241A had any effect. Login to comment

PMID: 16442101 [PubMed] Frelet A et al: "Insight in eukaryotic ABC transporter function by mutation analysis."

No. Sentence Comment

474 Other mutations either affected the transport of LTC4 and/or E217G (Y1243F) or reduced resistance to drugs (Y1236F, T1241A and Y1243F), suggesting that residues of the cytoplasmic half of TM17 with side chain hydrogen bonding potential participate in the formation of a substrate-binding site [218]. Login to comment

PMID: 16816140 [PubMed] Deeley RG et al: "Transmembrane transport of endo- and xenobiotics by mammalian ATP-binding cassette multidrug resistance proteins."

No. Sentence Comment

840 Despite the complete conservation of this region in MRP1, the only mutation that affected function was the conversion of Tyr1236 to Phe that selectively decreased resistance to vincristine (567) (Fig. 9). Login to comment
839 Despite the complete conservation of this region in MRP1, the only mutation that affected function was the conversion of Tyr1236 to Phe that selectively decreased resistance to vincristine (567) (Fig. 9). Login to comment
841 Despite the complete conservation of this region in MRP1, the only mutation that affected function was the conversion of Tyr1236 to Phe that selectively decreased resistance to vincristine (567) (Fig. 9). Login to comment

PMID: 17295059 [PubMed] Chang XB et al: "A molecular understanding of ATP-dependent solute transport by multidrug resistance-associated protein MRP1."

No. Sentence Comment

117 Many mutations in TM17, such as Y1236F, T1241A, T1242A, T1242C, T1242S, T1242L, Y1243F, N1245A, W1246C, W1246A, W1246F, W1246Y, or R1249K, significantly affect MRP1 function [83-86]. Login to comment

PMID: 19949927 [PubMed] Chang XB et al: "Molecular mechanism of ATP-dependent solute transport by multidrug resistance-associated protein 1."

No. Sentence Comment

104 Mutations of C43S in TM1 (112); P343A, K332L and K332D in TM6 (113, 114); W445A and P448A in TM8 (113, 115); T550A, T556A and P557A in TM10 (113, 116); N590A, F594A, P595A, N597A, S604A and S605A in TM11 (113, 117, 118); E1089Q, E1089A, E1089L, E1089N, K1092, S1097 and N1100 in TM14 (119, 120); R1197K in TM16 (121); Y1236F, T1241A, T1242A, T1242C, T1242S, T1242L, Y1243F, N1245A, W1246C, W1246A, W1246F, W1246Y or R1249K in TM17 (121-124) significantly affect MRP1 function. Login to comment