ABCC1 p.Glu1455Leu
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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).
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ABCC1 p.Glu1455Leu 10781583:33:96
status: NEW207 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.
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ABCC1 p.Glu1455Leu 10781583:207:124
status: NEW232 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.
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ABCC1 p.Glu1455Leu 10781583:232:135
status: NEW234 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.
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ABCC1 p.Glu1455Leu 10781583:234:135
status: NEW235 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).
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ABCC1 p.Glu1455Leu 10781583:235:245
status: NEW
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).
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ABCC1 p.Glu1455Leu 11741902:50:90
status: NEW117 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).
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ABCC1 p.Glu1455Leu 11741902:117:144
status: NEW118 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).
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ABCC1 p.Glu1455Leu 11741902:118:102
status: NEW173 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.
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ABCC1 p.Glu1455Leu 11741902:173:165
status: NEW175 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.
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ABCC1 p.Glu1455Leu 11741902:175:107
status: NEW180 F, influence of ATP on the [␣-32 P]8-N3ADP labeling of D1454L/E1455L.
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ABCC1 p.Glu1455Leu 11741902:180:69
status: NEW181 10 g of D1454L/E1455L was labeled in the presence of varying amounts of ATP indicated above each lane.
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ABCC1 p.Glu1455Leu 11741902:181:23
status: NEW
PMID: 12882957
[PubMed]
Payen LF et al: "Role of carboxylate residues adjacent to the conserved core Walker B motifs in the catalytic cycle of multidrug resistance protein 1 (ABCC1)."
No.
Sentence
Comment
78
The forward primers for D793Q, D793N, D793S, E1455Q, E1455N, E1455S, and E1455L were 5Ј-GCTGACATTTACCTCTTCGATCAACCGCTCTC- AGCAGTGGATGCC-3Ј, 5Ј-GCTGACATTTACCTCTTCGATAATCCGC- TCTCAGCAGTGGATGCC-3Ј, 5Ј-GCTGACATTTACCTCTTCGATTCT- CCCCTCTCAGCAGTGGATGCC-3Ј, 5Ј-CGAAGATCCTTGTGTTGGA- TCAGGCCACGGCGGCCGTGGACCTGG-3Ј, 5Ј-CGAAGATCCTTGTG- TTGGATA ACGCCACGGCCGCCGTGGACCTGG-3Ј, 5Ј-CGAAGATCC- TTGTGTTGGATTCGGCCACGGCAGCCGTGGACCTGG-3Ј, 5Ј-CGAA- GATCCTTGTGTTGGATTTGGCCACGGCCGCCGTGGACCTGG-3Ј, respectively.
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ABCC1 p.Glu1455Leu 12882957:78:73
status: NEW242 In addition, Glu1455 was mutated to Leu.
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ABCC1 p.Glu1455Leu 12882957:242:13
status: NEW249 In contrast, the NBD2 mutations (E1455S, E1455N, E1455Q, and E1455L) like E1455D completely abolished LTC4 transport (Fig. 7B).
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ABCC1 p.Glu1455Leu 12882957:249:61
status: NEW268 Like the E1455D mutant, the E1455S, E1455N, and E1455L mutations resulted in strong vanadate-independent photolabeling of NBD2 and increased vanadate-dependent photolabeling of NBD1 (Fig. 8C, lanes 3, 4, and 7-10).
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ABCC1 p.Glu1455Leu 12882957:268:48
status: NEW270 Effect of D793Q, D793N, D793S, E1455S, E1455Q, E1455N, E1455L mutations on [3 H]LTC4 transport activity.
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ABCC1 p.Glu1455Leu 12882957:270:55
status: NEW271 A, membrane proteins (1 g) from Sf21 cells expressing both halves of either MRP1 (MRP1 dh) or mutant proteins (D793Q, D793N, D793S, E1455S, E1455Q, E1455N, E1455L) were separated by SDS-PAGE on gradient gels and transferred to Immobilon-P membranes.
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ABCC1 p.Glu1455Leu 12882957:271:164
status: NEW275 B, membrane vesicles (2 g) containing MRP1 dh, D793Q, D793S, D793N, E1455Q, E1455S, E1455N, E1455L, or beta-Gus were assayed for ATP-dependent LTC4 transport activity at 23 °C for up to 3 min in transport buffer containing [3 H]LTC4 (50 nM, 0.13 Ci), as described under "Experimental Procedures."
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ABCC1 p.Glu1455Leu 12882957:275:100
status: NEW304 Comparison of nucleotide binding and vanadate trapping by wild-type MRP1 and mutant proteins (D793Q, D793N, D793S, E1455S, E1455Q, E1455N, and E1455L).
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ABCC1 p.Glu1455Leu 12882957:304:143
status: NEW305 A, at 4 °C, 8-azido- [␣-32 P]ATP photolabeling by wild-type MRP1 and mutant proteins (D793Q, D793N, D793S, E1455S, E1455Q, E1455N, and E1455L) was evaluated. Membrane vesicles (20 g) were incubated with 5 M 8-azido-[␣-32 P]ATP for 5 min on ice in transport buffer containing 5 mM MgCl2.
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ABCC1 p.Glu1455Leu 12882957:305:147
status: NEW308 The position of the labeled MRP1 NH2-half and COOH-half polypeptides are indicated, and endogenous proteins labeled are indicated by E followed by arrows. B and C, at 37 °C under trapping conditions, 8-azido-[␣-32 P]ADP trapping by wild-type MRP1 mutant proteins (D793Q, D793N, D793S, E1455S, E1455Q, E1455N, and E1455L) was studied.
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ABCC1 p.Glu1455Leu 12882957:308:325
status: NEW
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.
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ABCC1 p.Glu1455Leu 15737336:159:79
status: NEWX
ABCC1 p.Glu1455Leu 15737336:159:392
status: NEW
PMID: 17295059
[PubMed]
Chang XB et al: "A molecular understanding of ATP-dependent solute transport by multidrug resistance-associated protein MRP1."
No.
Sentence
Comment
245
For example, although ATPγS binding to wild-type or E1455D-mutated MRP1 significantly inhibited LTC4 labeling [62], ATPγS itself did not support the ATP-dependent LTC4 or E217βG transport [33, 47]; ATP can efficiently bind to E1455D, D793E/ E1455D or E1455L [62, 144], but mutation of this putative catalytic residue abolished the ATP-dependent solute transport [62, 144].
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ABCC1 p.Glu1455Leu 17295059:245:269
status: NEW261 This conclusion is further supported by mutation of the putative catalytic residue E1455 in NBD2 that all the mutants, including E1455S, E1455Q, E1455N, E1455L and E1455D, lost their abilities to transport LTC4 across membrane bilayer [62, 144].
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ABCC1 p.Glu1455Leu 17295059:261:153
status: NEW
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].
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ABCC1 p.Glu1455Leu 18088596:253:112
status: NEW254 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.
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ABCC1 p.Glu1455Leu 18088596:254:67
status: NEW
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.
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ABCC1 p.Glu1455Leu 18636743:12:124
status: NEW166 Indeed, elimination of the carboxyl group at D1454, such as D1454L/E1455L (8), had no effect on the protein folding and processing.
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ABCC1 p.Glu1455Leu 18636743:166:67
status: NEW
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.
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ABCC1 p.Glu1455Leu 19285030:163:99
status: NEW
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).
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ABCC1 p.Glu1455Leu 11469806:42:96
status: NEW147 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).
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ABCC1 p.Glu1455Leu 11469806:147:270
status: NEW174 Since hydrolysis is believed to drive MRP1 transport it would be expected that the mature D792A protein would not be capable of active transport.
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ABCC1 p.Glu1455Leu 11469806:174:293
status: NEW175 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).
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ABCC1 p.Glu1455Leu 11469806:175:293
status: NEW208 (G) K1333L, 0.3 ␮g protein in each lane.
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ABCC1 p.Glu1455Leu 11469806:208:11
status: NEW209 (H) D1454L/E1455L, 0.3 g protein in each lane.
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ABCC1 p.Glu1455Leu 11469806:209:11
status: NEW146 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).
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ABCC1 p.Glu1455Leu 11469806:146:270
status: NEW