ABCC7 p.Val510Cys
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PMID: 17911111
[PubMed]
Wang Y et al: "Correctors promote maturation of cystic fibrosis transmembrane conductance regulator (CFTR)-processing mutants by binding to the protein."
No.
Sentence
Comment
3
Although replacement of the 18 endogenous cysteines of CFTR with Ser or Ala yields a Cys-less mutant that does not mature at 37 °C, we found that maturation could be restored if Val510 was changed to Ala, Cys, Ser, Thr, Gly, Ala, or Asp.
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ABCC7 p.Val510Cys 17911111:3:183
status: NEW65 Fig. 2A shows that only the V510C mutation promoted maturation of Cys-less CFTR at 37 °C.
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ABCC7 p.Val510Cys 17911111:65:28
status: NEW70 Stable BHK cell lines expressing mutants V510A, V510C, V510S, V510G, or V510D were generated for use in iodide efflux assays.
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ABCC7 p.Val510Cys 17911111:70:48
status: NEW73 The results of mutants V510C, V510S, or V510G are not shown for clarity.
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ABCC7 p.Val510Cys 17911111:73:23
status: NEW82 ACCELERATED PUBLICATION: CFTR TM Domain Cross-linking 33248 To test whether the Val510 changes could also promote maturation of ⌬F508 CFTR (in a wild-type background), we introduced the Val510 mutations that promoted maturation of Cys-less CFTR (Val510 to Cys, Gly, Ala, Ser, Asp, or Thr) into ⌬F508 CFTR.
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ABCC7 p.Val510Cys 17911111:82:254
status: NEW
PMID: 18305154
[PubMed]
Serohijos AW et al: "Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function."
No.
Sentence
Comment
84
Nevertheless, the proximity or relative orientation of the F508C/F1068C, F508C/G1069C, and V510C/G1069C pairs permitted very little disulfide bond formation on oxidation catalyzed by copper phenanthroline, i.e., only a very small proportion of mature band was converted to cross-linked band Fig. 2.
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ABCC7 p.Val510Cys 18305154:84:91
status: NEW
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
51
We also constructed the V510C(NBD1)/A1067C(TMD2) CFTR mutant because position V510C or V510A promoted maturation of Cys-less CFTR (22).
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ABCC7 p.Val510Cys 18708637:51:78
status: NEW179 It was previously shown that mutations V510C or V510A promoted maturation of Cys-less CFTR (22).
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ABCC7 p.Val510Cys 18708637:179:39
status: NEW180 It was possible that V510C could interact with TMD2.
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ABCC7 p.Val510Cys 18708637:180:21
status: NEW
PMID: 19339490
[PubMed]
Wellhauser L et al: "A small-molecule modulator interacts directly with deltaPhe508-CFTR to modify its ATPase activity and conformational stability."
No.
Sentence
Comment
208
It is noteworthy that Loo et al. (2008) and Serohijos et al. (2008) showed that deletion of Phe508 impairs the chemical cross-linking that normally occurs between a non-native cysteine residue incorporated into NBD1, in the proximity of Phe508 (V510C), and a non-native cysteine introduced into the fourth intracellular loop (A1067C) Fig. 5.
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ABCC7 p.Val510Cys 19339490:208:245
status: NEW
PMID: 19761259
[PubMed]
Loo TW et al: "Correctors enhance maturation of DeltaF508 CFTR by promoting interactions between the two halves of the molecule."
No.
Sentence
Comment
11
Coexpression of ΔF508/N-half and C-half CFTR in the presence correctors VX-325 and corr-4a, however, restored interactions between the two halves. An interaction that was restored was that between NBD1 and TMD2 as the correctors restored cross-linking of mutant ΔF508/NBD1- (V510C)/TMD2(A1067C).
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ABCC7 p.Val510Cys 19761259:11:287
status: NEW48 The construction of double-cysteine CFTR mutant ΔF508/V510C- (NBD1)/A1067C(TMD2) in a Cys-less background was described previously (17).
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ABCC7 p.Val510Cys 19761259:48:60
status: NEW78 For example, mature CFTR shows cross-linking between cysteines in TM segment 6 (N-half) and TM segment 12 (C-half) or between cysteines in NBD1 [N-half (V510C)] and ICL4 [C-half (A1067C)], but the immature form of ΔF508 does not (17, 25).
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ABCC7 p.Val510Cys 19761259:78:153
status: NEW101 The black dot indicates the predicted location of an introduced cysteine (A1067C) in TMD2 that will directly cross-link to a cysteine introduced into NBD1 (V510C).
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ABCC7 p.Val510Cys 19761259:101:156
status: NEW
PMID: 20233947
[PubMed]
He L et al: "Restoration of domain folding and interdomain assembly by second-site suppressors of the DeltaF508 mutation in CFTR."
No.
Sentence
Comment
123
Cys- pair cross-linking also was not observed with Cys pairs at V510C/G1069C and K564C/G1069C in the NBD1/ CL4 interface of ⌬F508-CFTR (Fig. 3B).
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ABCC7 p.Val510Cys 20233947:123:64
status: NEW126 In addition, Cys pairs V510C/G1069C and K564C/G1069C at the NBD1/CL4 interface also were able to be cross-linked by M3M and M8M (Fig. 3B).
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ABCC7 p.Val510Cys 20233947:126:23
status: NEW181 Using this assay, we compared the accessibility of 491C and V510C in NBD1 of full-length CFTR in the absence or presence of ⌬F508.
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ABCC7 p.Val510Cys 20233947:181:60
status: NEW202 In contrast to the buried 491C, V510C was clearly labeled in both immature and mature forms of WT-CFTR (lane 5).
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ABCC7 p.Val510Cys 20233947:202:32
status: NEW205 This may reflect the involvement of this loop in the NBD1/CL4 interface, as shown with the cross-linking of V510C/ G1069C in the mature but not in the immature form (18).
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ABCC7 p.Val510Cys 20233947:205:108
status: NEW206 In contrast to the more buried 491C, introduction of ⌬F508 did not make V510C more accessible to labeling compared to the immature WT-CFTR (lane 6).
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ABCC7 p.Val510Cys 20233947:206:79
status: NEW207 Introduction of the suppressor mutations did not appear to reduce exposure of V510C in the immature form, as it had the more buried 491C.
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ABCC7 p.Val510Cys 20233947:207:78
status: NEW208 However, the accessibility of V510C in the mature form, which was restored by the suppressors, was similar to that in the WT-CFTR (lane 7).
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ABCC7 p.Val510Cys 20233947:208:30
status: NEW
PMID: 20561529
[PubMed]
Aleksandrov AA et al: "Regulatory insertion removal restores maturation, stability and function of DeltaF508 CFTR."
No.
Sentence
Comment
154
HEK 293 cells were transiently transfected with Cys-less ΔF508 CFTR with Cys pairs introduced at the CL2-NBD2 (C276-Q1280C) or CL4-NBD1 (V510C-G1069C) interfaces in the absence or presence of ΔRI.
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ABCC7 p.Val510Cys 20561529:154:143
status: NEW
PMID: 20590134
[PubMed]
Loo TW et al: "The V510D suppressor mutation stabilizes DeltaF508-CFTR at the cell surface."
No.
Sentence
Comment
178
While introduction of V510D into Cys-less or ΔF508-CFTRs promoted maturation, the Cys-less mutant was different because its maturation could also be promoted by changing Val510 to Thr, Cys, Gly, Ala, or Ser.
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ABCC7 p.Val510Cys 20590134:178:176
status: NEW
PMID: 21520952
[PubMed]
Loo TW et al: "Benzbromarone stabilizes DeltaF508 CFTR at the cell surface."
No.
Sentence
Comment
30
Figure 1C shows that 50 μM benzbromarone inhibited cross-linking between TMD1 and TMD2 [M348C(TM6)/ T1142C(TM12)] but not between NBD1 and TMD2 [V510C- (NBD1)/A1067C(ICL4)].
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ABCC7 p.Val510Cys 21520952:30:151
status: NEW50 (C) Effect of benzbromarone on cross-linking (X-link) between cysteines in TMD1 and TMD2 (M348C/T1142C) or NBD1 and TMD2 (V510C/A1067C).7 (D) Immunoblot of cells expressing CFTR TMD1þ2 in the absence (À) or presence (þ) of 0.05 mM benzbromarone.
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ABCC7 p.Val510Cys 21520952:50:122
status: NEW
PMID: 21594776
[PubMed]
Loo TW et al: "Repair of CFTR folding defects with correctors that function as pharmacological chaperones."
No.
Sentence
Comment
252
The following protocols describe disulfide cross-linking between cysteines introduced into NBD1 (V510C) and the fourth intracellular loop in TMD2 (A1067C) of a F508del-CFTR processing mutant expressed in the presence or the absence of correctors.
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ABCC7 p.Val510Cys 21594776:252:97
status: NEW263 The next day, add 0.17 mg of (V510C)/(A1067C)/ F508del-CFTR cDNA to sterile water to give a total volume of 7.65 ml.
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ABCC7 p.Val510Cys 21594776:263:30
status: NEW282 Effect of correctors on cross-linking of CFTR mutant F508del/V510C (NBD1)/A1067C(TMD2).
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ABCC7 p.Val510Cys 21594776:282:61
status: NEW
PMID: 15581632
[PubMed]
Buyse F et al: "Mistargeted MRPdeltaF728 mutant is rescued by intracellular GSH."
No.
Sentence
Comment
154
HEK 293 cells were transiently transfected with Cys-less ΔF508 CFTR with Cys pairs introduced at the CL2-NBD2 (C276-Q1280C) or CL4- NBD1 (V510C-G1069C) interfaces in the absence or presence of ΔRI.
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ABCC7 p.Val510Cys 15581632:154:144
status: NEW
PMID: 22406676
[PubMed]
Aleksandrov AA et al: "Allosteric modulation balances thermodynamic stability and restores function of DeltaF508 CFTR."
No.
Sentence
Comment
155
Using an otherwise Cys-less construct, we had previously observed methanethiosulfonate-mediated cross-linking between V510C and G1069C in WT CFTR.29,33 Figure 7 shows similar cross-linking of this pair of residues in ΔF/4PT CFTR, providing evidence that the stabilization of ΔF508 NBD1 can Fig. 6.
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ABCC7 p.Val510Cys 22406676:155:118
status: NEW178 HEK293 cells were transiently transfected with Cys-less CFTR or Cys-less ΔF508-CFTR in the presence or absence of the 4PT mutations (S422P/S434P/S492P/A534P/I539T), with the Cys pair V510C/G1069C introduced at the CL4/NBD1 interface.
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ABCC7 p.Val510Cys 22406676:178:188
status: NEW279 Briefly, HEK cells transiently expressing Cys-less CFTR constructs with V510C and G1069C substitutions on the WT or ΔF/4PT CFTR basis grown on 35-mm tissue culture dishes were harvested, washed twice in PBS, and resuspended in 60 μl of PBS.
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ABCC7 p.Val510Cys 22406676:279:72
status: NEW
PMID: 23104983
[PubMed]
He L et al: "Correctors of DeltaF508 CFTR restore global conformational maturation without thermally stabilizing the mutant protein."
No.
Sentence
Comment
126
HEK293 cells were transiently transfected with Cys-less CFTR or Cys-less èc;F508 CFTR with Cys pairs 276C/Q1280C or V510C/G1069C, introduced at NBD2/CL2 and NBD1/CL4 interfaces, respectively (13).
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ABCC7 p.Val510Cys 23104983:126:120
status: NEW