ABCC2 p.Lys578Ala
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PMID: 16442101
[PubMed]
Frelet A et al: "Insight in eukaryotic ABC transporter function by mutation analysis."
No.
Sentence
Comment
491
HsMRP2 Replacement of basic residues (K324 (TM6), K483 (TM9), R1210 (TM16) and R1257 (TM17)) with alanine decreased the ability to transport an organic anion substrate, glutathione-methlyfluorescein and K578A resulted in decreased protein expression.
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ABCC2 p.Lys578Ala 16442101:491:203
status: NEW
PMID: 10978330
[PubMed]
Ryu S et al: "Identification of basic residues involved in drug export function of human multidrug resistance-associated protein 2."
No.
Sentence
Comment
3
Four mutants, K324A (TM6), K483A (TM9), R1210A (TM16), and R1257A (TM17), showed decreased transport activity, and another mutant, K578A (TM11), showed decreased protein expression.
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ABCC2 p.Lys578Ala 10978330:3:131
status: NEW42 Site-directed Mutagenesis-The seven mutants of MRP2, K316A, K324A, K329A, H439A, K483A, K578A, and R590A, were generated by the overlapping polymerase chain reaction method.
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ABCC2 p.Lys578Ala 10978330:42:88
status: NEW96 Except for K578A, all of the mutants were expressed at nearly the same level when compared with wild type MRP2.
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ABCC2 p.Lys578Ala 10978330:96:11
status: NEW112 The experiments Only the expression of K578A was faint in both immunoblot and immunocytochemistry.
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ABCC2 p.Lys578Ala 10978330:112:40
status: NEW118 As to K578A mutant, GS-MF excretion decreased to the level of control (Fig. 8); however, expression level of this mutant also decreased (Figs. 5 and 6).
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ABCC2 p.Lys578Ala 10978330:118:6
status: NEW121 As shown in Fig. 10, we observed with confocal fluorescence microscopy that these mutant MRP2s including K578A were expressed at the cell surface.
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ABCC2 p.Lys578Ala 10978330:121:105
status: NEW122 Therefore, the defect in the transport function of these mutants was clearly due to the functional defect except for K578A.
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ABCC2 p.Lys578Ala 10978330:122:117
status: NEW123 The decrease in transport activity of K578A was mainly due to the decrease in the expression level.
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ABCC2 p.Lys578Ala 10978330:123:38
status: NEW147 Except for a mutant K578A, the protein expression level of these mutants in COS-7 cell was comparable with that of wild type (Figs. 5 and 6).
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ABCC2 p.Lys578Ala 10978330:147:20
status: NEW148 Among these mutants, K578A, R1210A, and R1257A were the most influenced by mutation concerning substrate translocating activity FIG. 6.
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ABCC2 p.Lys578Ala 10978330:148:21
status: NEW161 As to K578A, the excretion of GS-MF and protein expression was coincidentally lowered (Figs. 5, 6, and 8).
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ABCC2 p.Lys578Ala 10978330:161:6
status: NEW