ABCC1 p.Asp336Arg
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PMID: 12186871
[PubMed]
Haimeur A et al: "Charged amino acids in the sixth transmembrane helix of multidrug resistance protein 1 (MRP1/ABCC1) are critical determinants of transport activity."
No.
Sentence
Comment
47
The sequences of the individual sense strands, with the altered codons underlined and the corresponding changes in amino acids indicated in parentheses were as follows: (K332D) 5Ј-CTC ATG AGC TTC TTC TTC GAC GCC ATC CAC GAC CTG-3Ј; (K332L) 5Ј-CTC ATG AGC TTC TTC TTC CTG GCC ATC CAC GAC CTG-3Ј; (H335E) 5Ј-GC TTC TTC TTC AAG GCC ATC GAG GAC CTG ATG ATG-3Ј; (H335L) 5Ј-GC TTC TTC TTC AAG GCC ATC TTG GAC CTG ATG ATG-3Ј; (H335Q) 5Ј-GC TTC TTC TTC AAG GCC ATC CAG GAC CTG ATG ATG-3Ј; (D336R) 5Ј-C AAG GCC ATC CAC CGG CTG ATG ATG TTT TCG-3Ј; (D336L) 5Ј-C AAG GCC ATC CAC CTG CTG ATG ATG TTT TCG-3Ј.
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ABCC1 p.Asp336Arg 12186871:47:542
status: NEW104 Representative confocal micrographs of cells expressing GFP-tagged wild-type MRP1 and mutants K332D, H335E, and D336R are shown in Fig. 2.
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ABCC1 p.Asp336Arg 12186871:104:112
status: NEW106 In the case of the MRP1-Lys332 mutants K332D and K332L (Fig. 3B) and the MRP1-Asp336 mutants D336L and D336R (Fig. 3D), LTC4 uptake was reduced to levels that were indistinguishable from those observed with vesicles prepared from empty vector-transfected control cells.
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ABCC1 p.Asp336Arg 12186871:106:103
status: NEW125 In contrast, substitution of Asp336 with either Leu or Arg led to a complete loss of E217betaG uptake.
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ABCC1 p.Asp336Arg 12186871:125:29
status: NEW126 Thus, as shown in Fig. 5C, MRP1-Asp336 mutants D336L and D336R exhibited the same E217betaG uptake activity as the empty vector control.
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ABCC1 p.Asp336Arg 12186871:126:57
status: NEW142 D, wild-type MRP1 (f), MRP1 mutants D336L (Œ) and D336R (‚), and control empty pcDNA3.1(-) vector (E).
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ABCC1 p.Asp336Arg 12186871:142:56
status: NEW152 However, this band is not detectable in [3 H]LTC4 photolabeled proteins from cells expressing comparable levels of the MRP1 mutants K332D and K332L or mutants D336L and D336R, indicating that these mutations abrogate photolabeling and hence binding of this compound.
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ABCC1 p.Asp336Arg 12186871:152:169
status: NEW165 C, time courses of [3 H]E217betaG uptake by membrane vesicles prepared from HEK293T cells transfected with cDNAs encoding wild-type MRP1 (f), TM6 mutants D336L (Œ), and D336R (‚), and the empty pcDNA3.1(-) vector control (E).
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ABCC1 p.Asp336Arg 12186871:165:175
status: NEW177 Substitution of Asp336 with Leu (D336L) reduced GSH uptake to ϳ25% of wild-type MRP1 levels, whereas substitution of this negatively charged residue with a positively charged residue (D336R) further reduced uptake of this tripeptide to just above basal levels observed with vesicles from the empty vector control (Fig. 7C).
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ABCC1 p.Asp336Arg 12186871:177:190
status: NEW185 In contrast, MTX uptake was reduced by ϳ50% when Asp336 was substituted with Leu (D336L) and by ϳ65% when substituted with Arg (D336R) (not shown).
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ABCC1 p.Asp336Arg 12186871:185:140
status: NEW204 Membrane vesicles were preincubated with acivicin and then incubated with [3 H]GSH in the presence of 30 M apigenin in transport buffer for 20 min at 37 °C. A, K332D and K332L; B, H335E, H335L, and H335Q; C, D336L and D336R.
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ABCC1 p.Asp336Arg 12186871:204:231
status: NEW208 F, WT-MRP1 (f); D336L (Œ); D336R (‚); vector control (E).
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ABCC1 p.Asp336Arg 12186871:208:33
status: NEW217 Substitutions of MRP1-Asp336 had a more dramatic effect on MRP1 transport activity than substitutions of either Lys332 or His335 in that the D336L and D336R mutants did not transport four of the five organic anion substrates tested, and transport of the fifth, MTX, was reduced by at least 50%.
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ABCC1 p.Asp336Arg 12186871:217:151
status: NEW
PMID: 15155831
[PubMed]
Haimeur A et al: "Mutations of charged amino acids in or near the transmembrane helices of the second membrane spanning domain differentially affect the substrate specificity and transport activity of the multidrug resistance protein MRP1 (ABCC1)."
No.
Sentence
Comment
5
The overall organic anion transport activity of the same-charge mutant of Asp336 (D336E) also remained very low, as observed for D336R.
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ABCC1 p.Asp336Arg 15155831:5:129
status: NEW123 In our earlier study, we showed that substitution of the negatively charged TM6 Asp336 residue with Arg or Leu essentially eliminated the transport of both conjugated and unconjugated MRP1 organic anion substrates (Haimeur et al., 2002).
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ABCC1 p.Asp336Arg 15155831:123:80
status: NEW