ABCC7 p.Leu1260Ala
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PMID: 18708637
[PubMed]
Loo TW et al: "Processing mutations disrupt interactions between the nucleotide binding and transmembrane domains of P-glycoprotein and the cystic fibrosis transmembrane conductance regulator (CFTR)."
No.
Sentence
Comment
47
The G268V and L1260A processing mutations were introduced into the L443C(NBD1)/S909C(TMD2) mutant.
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ABCC7 p.Leu1260Ala 18708637:47:14
status: NEW108 The locations of processing mutations G268V and L1260A that were used to inhibit maturation of P-gp are indicated as squares.
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ABCC7 p.Leu1260Ala 18708637:108:48
status: NEW136 To test if NBD-TMD2 interactions differ in the mature and immature forms of P-gp, the G268V (26) or L1260A (38) processing mutations were introduced into mutant L443C(NBD1)/ S909C(TMD2) to inhibit its maturation.
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ABCC7 p.Leu1260Ala 18708637:136:100
status: NEW140 The G268V mutation is located in the second intracellular loop in TMD1 whereas the L1260A mutation is located at the COOH-end of NBD2.
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ABCC7 p.Leu1260Ala 18708637:140:83
status: NEW159 Mutants G268V/L443C(NBD1)/S909C(TMD2) and L1260A/L443C(NBD1)/S909C(TMD2) were expressed in HEK 293 cells in the presence of no drug (None) or 10 m cyclosporin A (ϩ Cyclo).
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ABCC7 p.Leu1260Ala 18708637:159:42
status: NEW166 B, mutant A266C(TMD1)/F1086C(NBD2) containing the L1260A processing mutation was expressed in HEK 293 cells in the absence (no drug) or presence of 10 M cyclosporin A (ϩ Cyclo).
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ABCC7 p.Leu1260Ala 18708637:166:50
status: NEW171 To test if there were structural differences between the mature and immature forms of P-gp at the TMD1-NBD2 interface, the L1260A processing mutation was introduced into mutant A266C(TMD1)/F1086C(NBD2).
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ABCC7 p.Leu1260Ala 18708637:171:123
status: NEW172 Mutant L1260A/ A266C(TMD1)/F1086C(NBD2) was expressed in the presence or absence of cyclosporin A and membranes prepared from the cells were treated with or without copper phenanthroline at 0 °C followed by immunoblot analysis. Fig. 6B shows that cross-linking was observed with mature P-gp (right panel) but not with immature P-gp (left panel).
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ABCC7 p.Leu1260Ala 18708637:172:7
status: NEW199 Processing mutations near the NH2- (G268V) or COOH-end (L1260A) of the molecule disrupted cross-linking between Cys-443(NBD1) and Cys-909(TMD2).
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ABCC7 p.Leu1260Ala 18708637:199:56
status: NEW202 Studies on the L1260A/ A266C(TMD1)/F1086C(NBD2) mutant showed that only the mature form of the protein could undergo cross-linking (Fig. 6B).
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ABCC7 p.Leu1260Ala 18708637:202:15
status: NEW210 The presence of a processing mutation such as L1260A traps P-gp as immature protein with incomplete NBD-TMD contacts (Fig. 8, left panel).
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ABCC7 p.Leu1260Ala 18708637:210:46
status: NEW
PMID: 21182301
[PubMed]
Loo TW et al: "The W232R suppressor mutation promotes maturation of a truncation mutant lacking both nucleotide-binding domains and restores interdomain assembly and activity of P-glycoprotein processing mutants."
No.
Sentence
Comment
57
The red balls show the locations of Trp232 and the processing mutations at positions 251 (G251V), 490 (ΔY490), 709 (P709A), 722 (G722A), and 1260 (L1260A).
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ABCC7 p.Leu1260Ala 21182301:57:153
status: NEW67 Mutations were introduced into wild-type P-gp or processing mutants containing processing mutations in different domains (G251V in TMD1, ΔY490 in NBD1, P709A in the linker region, G722A in TMD2, or L1260A in NBD2) as described previously (28).
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ABCC7 p.Leu1260Ala 21182301:67:204
status: NEW91 The G251V or L1260A processing mutations were introduced into Cys-less P-gp containing pairs of cysteines in different domains (L443C(NBD1)/ S909C(TMD2), L531C(NBD1)/C1074(NBD2), or C137(TMD1)/A935C(TMD2)) with or without the W232R mutation.
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ABCC7 p.Leu1260Ala 21182301:91:13
status: NEW92 The L1260A and L1260A/W232R mutations were also introduced into a Cys-less P-gp containing the A266C(TMD1)/ F1086C(NBD2) mutations.
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ABCC7 p.Leu1260Ala 21182301:92:4
status: NEWX
ABCC7 p.Leu1260Ala 21182301:92:15
status: NEW125 The W232R mutation was introduced into mutants P709A (linker region), G722A (TMD2), or L1260A (NBD2).
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ABCC7 p.Leu1260Ala 21182301:125:87
status: NEW155 To test if the W232R mutation restored domain-domain contacts, it was introduced into the G251V or L1260A processing mutants that also contained pairs of cysteines at the TMD1-TMD2 (C137(TMD1)/A935C(TMD2), NBD1-NBD2 (L531C(NBD1)/C1074(NBD2), or NBD1-TMD2 (L443C(NBD1)/S909C(TMD2) interfaces.
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ABCC7 p.Leu1260Ala 21182301:155:99
status: NEW156 The G251V and L1260A parents were used because the G251V mutation is in the same domain as W232R (TMD1) whereas L1260A is in another domain (NBD2).
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ABCC7 p.Leu1260Ala 21182301:156:14
status: NEWX
ABCC7 p.Leu1260Ala 21182301:156:112
status: NEW158 Introduction of the W232R mutation into all of the G251V (Figure 3A, lanes 3, 7, and 11) or L1260A (Figure 3B, lanes 3, 7, and 11) double-cysteine processing mutants restored maturation.
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ABCC7 p.Leu1260Ala 21182301:158:92
status: NEW162 Since the L1260A mutation is located in the NBD2 (Figure 1A), we also examined the effects of W232R on NBD2-TMD1 interactions.
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ABCC7 p.Leu1260Ala 21182301:162:10
status: NEW164 Accordingly, we introduced the W232R mutation into mutant A266C/F1086C/L1260A.
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ABCC7 p.Leu1260Ala 21182301:164:71
status: NEW166 Figure 3C shows that the W232R mutation promoted maturation of the mutant A266C/F1086C/L1260A (lane 3) and that only the mature protein was cross-linked (lane 4).
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ABCC7 p.Leu1260Ala 21182301:166:87
status: NEW187 Membranes were prepared from cells expressing P-gp processing mutants G251V ( W232R (A) or L1260A ( W232R (B) that also contained pairs of cysteines in various domains (L443C(NBD1)/S909C(TMD2), L531C(NBD1)/C1074(NBD2), C137(TMD1)/A935C(TMD2)).
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ABCC7 p.Leu1260Ala 21182301:187:91
status: NEW188 Membranes were also prepared from cells expressing the L1260A processing mutant ( W232R containing cysteines in TMD1 and NBD2 (A266C/F1086C) (C).
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ABCC7 p.Leu1260Ala 21182301:188:55
status: NEW
PMID: 16926162
[PubMed]
Loo TW et al: "Insertion of an arginine residue into the transmembrane segments corrects protein misfolding."
No.
Sentence
Comment
81
The I306R mutation was introduced into mutants containing a processing mutation in the TM segments (G300V in TM5, G722A in TM7), the loops connecting the TM segments (G251V in intracellular loop 2, F804A in intracellular loop 3), the linker region (P709A), and NBD2 (L1260A) (Fig. 1A).
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ABCC7 p.Leu1260Ala 16926162:81:267
status: NEW83 The I306R mutation was more efficient, however, in promoting maturation of mutants G251V, G300V, P709A, and G722A than mutants F804A and L1260A.
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ABCC7 p.Leu1260Ala 16926162:83:137
status: NEW100 A, immunoblot analysis of whole cell extracts of HEK 293 cells expressing the A52-tagged P-gp processing mutants G251V, G300V, P709A, G722A, F804A, and L1260A with or without the I306R mutation.
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ABCC7 p.Leu1260Ala 16926162:100:152
status: NEW
PMID: 25987565
[PubMed]
Loo TW et al: "The Transmission Interfaces Contribute Asymmetrically to the Assembly and Activity of Human P-glycoprotein."
No.
Sentence
Comment
317
For example the CFTR N1303K (54) and P-gp L1260A (55) NBD2 mutations inhibit maturation of the proteins.
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ABCC7 p.Leu1260Ala 25987565:317:42
status: NEW