ABCC1 p.Ser605Ala
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PMID: 15260484
[PubMed]
Zhang DW et al: "Transmembrane helix 11 of multidrug resistance protein 1 (MRP1/ABCC1): identification of polar amino acids important for substrate specificity and binding of ATP at nucleotide binding domain 1."
No.
Sentence
Comment
7
N597A increased and decreased resistance to vincristine and VP-16, respectively, while S605A decreased resistance to vincristine, VP-16 and doxorubicin.
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ABCC1 p.Ser605Ala 15260484:7:87
status: NEW55 Mutations Q580A, T581A, S604T, and S605A were generated using the Transformer- Site-Directed Mutagenesis kit (CLONTECH, Palo Alto, CA).
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ABCC1 p.Ser605Ala 15260484:55:35
status: NEW59 They are as follows: Q580A (5'-C ATC CTG GAT GCC GCG ACG GCC TTC GTG TC-3'), T581A (5'-CTG GAT GCC CAG GCG GCC TTC GTG TCT TTG-3'), S605A (5'-C ATG GTC ATC AGC GCG ATC GTG CAG GCG-3'), and S604T (5'-CCC ATG GTC ATC ACT AGT ATC GTG CAG GCG-3').
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ABCC1 p.Ser605Ala 15260484:59:132
status: NEW151 The levels of LTC4 uptake by vesicles prepared from HEK transfectants expressing either wild-type MRP1 or mutations Q580A, T581A, S585A, N597A, S604A, and S605A were proportional to the relative expression levels of the wild-type and mutant proteins.
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ABCC1 p.Ser605Ala 15260484:151:155
status: NEW154 Mutations Q580A, T581A, S585A, N597A, and S605A had no detectable effect on transport.
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ABCC1 p.Ser605Ala 15260484:154:42
status: NEW206 Replacement of Ser605 by Ala also resulted in approximately a 2-3-fold reduction of resistance to all three drugs tested.
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ABCC1 p.Ser605Ala 15260484:206:15
status: NEW216 In contrast, mutations N597A and S605A influenced only the drug resistance profile of MRP1, and mutation S604A affected the transport of only E217 G.
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ABCC1 p.Ser605Ala 15260484:216:33
status: NEW221 Other mutations, including N597A and S605A, which influenced MRP1-mediated drug resistance, had no effect, suggesting that they modify interactions between MRP1 and the drug rather than altering the ability to bind and transport GSH.
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ABCC1 p.Ser605Ala 15260484:221:37
status: NEW272 On the other hand, mutation of Ser605 to Ala decreased the ability of MRP1 to confer resistance to vincristine, VP-16, and doxorubicin, consistent with our previous proposal that hydrogen bonding may be a common form of interaction between MRP1 and its substrates (30-33, 45, 55, 60).
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ABCC1 p.Ser605Ala 15260484:272:31
status: NEW273 In addition, mutations N597A and S605A affected only the drug-resistance profile of MRP1.
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ABCC1 p.Ser605Ala 15260484:273:33
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
112
Many mutations in TM11, such as N590A, F594A, N597A, S604A and S605A, also modulate the drug resistance profile of MRP1 [79, 80].
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ABCC1 p.Ser605Ala 17295059:112:63
status: NEW
PMID: 18612080
[PubMed]
El-Sheikh AA et al: "Functional role of arginine 375 in transmembrane helix 6 of multidrug resistance protein 4 (MRP4/ABCC4)."
No.
Sentence
Comment
215
Deletion of the hydroxyl group of MRP1 residue 605 (S605A), corresponding to R375A in MRP4, decreased resistance to vincristine, etoposide (VP-16), and doxorubicin (Zhang et al., 2004).
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ABCC1 p.Ser605Ala 18612080:215:52
status: NEW
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.
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ABCC1 p.Ser605Ala 19949927:104:190
status: NEW