ABCMdb

ABCC1 p.Asp1454Leu

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Publications

PMID: 10781583 [PubMed] Hou Y et al: "Allosteric interactions between the two non-equivalent nucleotide binding domains of multidrug resistance protein MRP1."

No. Sentence Comment

33 Stable cell lines expressing wild-type and mutant MRP1s, K684L, D792L/D793L, K1333L, and D1454L/E1455L, were generated by using procedures described previously (11). Login to comment
205 Fig. 5C shows that although labeling by N3[␣-32 P]ATP was not abolished by the mutations, it was greatly reduced: K684L was ϳ10% of wild-type; K1333L, ϳ5%; D1454L/D1455L, ϳ15%. Login to comment
207 Fig. 5D demonstrates that labeling of K684L by N3[␥-32 P]ATP was almost eliminated and labeling of K1333L and D1454L/E1455L were decreased to ϳ10% and ϳ15% of the wild-type levels, respectively. Login to comment
232 Lane 1, 10 ␮g of wild-type MRP1; lane 2, 20 ␮g of K684L; lane 3, 10 ␮g of K1333L; lane 4, 10 ␮g of D1454L/ E1455L. Login to comment
234 Lane 1, 10 ␮g of wild-type MRP1; lane 2, 20 ␮g of K684L; lane 3, 10 ␮g of K1333L; lane 4, 10 ␮g of D1454L/ E1455L. Login to comment
235 E, ATP-dependent LTC4 uptake by membrane vesicles containing wild-type (closed diamonds) and mutant MRPs: NBD1 Walker A lysine mutant K684L (open circles), NBD2 Walker A lysine mutant K1333L (open square), NBD2 Walker B aspartate mutant D1454L/ E1455L (closed circles). Login to comment

PMID: 11741902 [PubMed] Hou YX et al: "ATP binding to the first nucleotide-binding domain of multidrug resistance protein MRP1 increases binding and hydrolysis of ATP and trapping of ADP at the second domain."

No. Sentence Comment

50 Stable cell lines expressing wild-type and mutant MRP1s, K684L, D792A, K1333L, and D1454L/E1455L were established previously (2, 31). Login to comment
117 Essentially the stimulation was much reduced in the NBD1 mutants, K684L and D792A (Fig. 4, C and D), and in the NBD2 mutants, K1333L and D1454L/E1455L (Fig. 4, E and F), and the stimulation effects were shifted to higher ATP concentrations (Fig. 4, C-F). Login to comment
118 Trypsin digestion of either [␣-32 P]8-N3ATP or [␣-32 P]8N3ADP-labeled K1333L and D1454L/E1455L proved that the mutated NBD2 fragment can still be labeled (data not shown). Login to comment
173 Lane 1, 10 ␮g of wild-type MRP1; lane 2, 15 ␮g of K684L; lane 3, 20 ␮g of D792A; lane 4, 10 ␮g of K1333L; lane 5, 10 ␮g of D1454L/E1455L. Login to comment
175 The results for K684L and D792A are the average of three independent experiments and for K1333L and D1454L/E1455L are the average of two independent experiments. C, influence of ATP on the [␣-32 P]8-N3ADP labeling of K684L. Login to comment
180 F, influence of ATP on the [␣-32 P]8-N3ADP labeling of D1454L/E1455L. Login to comment
181 10 ␮g of D1454L/E1455L was labeled in the presence of varying amounts of ATP indicated above each lane. Login to comment

PMID: 15737336 [PubMed] Yang R et al: "Nucleotide dissociation from NBD1 promotes solute transport by MRP1."

No. Sentence Comment

159 Interestingly, this result is also similar to that of the double mutant D1454L/E1455L [28] including the mutations of the D1454 residue in the Walker B motif and the putative catalytic base E1455 residue directly adjacent to the D1454, implying that the mutation of the putative catalytic base E1455 to a non-acidic amino acid affecting ATP hydrolysis [43] has the same effects as the D1454L/E1455L double mutant affecting ATP binding [28] and hydrolysis. Login to comment

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

No. Sentence Comment

160 D792A (NBD1) and D1454L/E1455L (NBD2) diminished nucleotide-binding abilities rather than completely abolishing binding [100]. Login to comment

PMID: 18088596 [PubMed] Yang R et al: "The hydroxyl group of S685 in Walker A motif and the carboxyl group of D792 in Walker B motif of NBD1 play a crucial role for multidrug resistance protein folding and function."

No. Sentence Comment

253 In addition, substitutions of the Walker B motif D1454 and E1455 in NBD2 of MRP1 with a leucine residue (D1454L/E1455L) also did not cause misfolding of the protein [20]. Login to comment
254 In order to rule out the possibility that the double mutant D1454L/E1455L might rescue the misfolding caused by D14 54L mutation, we have made single mutants including D1454L, D1454N, S1334A, S1334T, S1334C, S1334H, S1334D and S1334N. Login to comment
261 It is also true for the corresponding mutations in Walker B motif of NBD2 in MRP1, such as D1454L (manuscript in preparation) and D1454N [46], have a significant effect on the ATP-dependent LTC4 transport. Login to comment

PMID: 18636743 [PubMed] Yang R et al: "Interaction between the bound Mg.ATP and the Walker A serine residue in NBD2 of multidrug resistance-associated protein MRP1 plays a crucial role for the ATP-dependent leukotriene C4 transport."

No. Sentence Comment

12 In contrast, however, substitution of the corresponding Walker B D1454 in NBD2 with the hydrophobic residue leucine (D1454L/E1455L) did not cause misfolding of the mutated MRP1 protein (8), suggesting distinct structures in NBD1 and NBD2 of MRP1. Login to comment
166 Indeed, elimination of the carboxyl group at D1454, such as D1454L/E1455L (8), had no effect on the protein folding and processing. Login to comment

PMID: 19285030 [PubMed] Wan L et al: "Characterization of the ATPase activity of a novel chimeric fusion protein consisting of the two nucleotide binding domains of MRP1."

No. Sentence Comment

163 Among the NBD1-GST-NBD2 mutants, K684L in Walker A of NBD1, K1333L in Walker A of NBD2, and D1454L/E1455L in Walker B of NBD2 were expressed mainly as inclusion bodies in E. coli, and only the E1455Q mutant was expressed in a sufficient quantity of soluble protein to allow activity analysis. Login to comment

PMID: 11469806 [PubMed] Cui L et al: "Mutations of the Walker B motif in the first nucleotide binding domain of multidrug resistance protein MRP1 prevent conformational maturation."

No. Sentence Comment

42 Stable cell lines expressing wild-type and mutant MRP1s, K684L, D792L/D793L, K1333L, and D1454L/E1455L were established previously (8). Login to comment
147 This was also true in the case of D793L (Fig. 5E) and mutations of the Walker A lysine residues in both NBDs (Fig. 5B, K684L, and Fig. 5G, K1333L), where the protein matured normally as did a variant in which the Walker B aspartate in NBD2 was mutated (Fig. 5H, D1454L/ E1455L). Login to comment
174 Since hydrolysis is believed to drive MRP1 transport it would be expected that the mature D792A protein would not be capable of active transport. Login to comment
175 The data in Fig. 7 confirm this expectation, i.e., there is not significantly more ATP-dependent LTC4 uptake by vesicles containing D792A protein that does mature than by the other variants that do not mature (Fig. 7, D792L and D792L/D793L), nor by the NBD2 mutants (Fig. 7, K1333L and D1454L/E1455L) that do mature but have difficulties to hydrolyze ATP and to trap the hydrolysis product, ADP (8). Login to comment
208 (G) K1333L, 0.3 ␮g protein in each lane. Login to comment
209 (H) D1454L/E1455L, 0.3 ␮g protein in each lane. Login to comment
146 This was also true in the case of D793L (Fig. 5E) and mutations of the Walker A lysine residues in both NBDs (Fig. 5B, K684L, and Fig. 5G, K1333L), where the protein matured normally as did a variant in which the Walker B aspartate in NBD2 was mutated (Fig. 5H, D1454L/ E1455L). Login to comment