ABCC7 p.Arg104Glu
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PMID: 18449561
[PubMed]
Zhou JJ et al: "Identification of positive charges situated at the outer mouth of the CFTR chloride channel pore."
No.
Sentence
Comment
60
As shown in Fig. 2, similar inward rectification is observed in the charge-reversing mutants R104E, R117E, and K335E and to a much lesser extent, R1128E, under symmetrical ionic conditions in excised membrane patches.
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ABCC7 p.Arg104Glu 18449561:60:93
status: NEW67 In contrast to the linear I-V relationship seen in wild-type CFTR with symmetrical 154 mM Cl- solutions, mutants R104E, R117E, and K335E showed clear inward rectification.
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ABCC7 p.Arg104Glu 18449561:67:113
status: NEW73 As shown in Fig. 3b, macroscopic current rectification was indeed sensitive to symmetrical Cl-concentration in R104E, R117E, and K335E, being more pronounced at low Cl-concentration.
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ABCC7 p.Arg104Glu 18449561:73:111
status: NEW79 However, current amplitude was significantly reduced in R104E, R117E, and K335E (Fig. 4a, b).
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ABCC7 p.Arg104Glu 18449561:79:56
status: NEW91 All mutants depicted (R104Q, R117Q, K335A, R1128Q, R104E, R117E, K335E, R1128E) showed rectification ratios significantly different from wild type (asterisk P<0.05).
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ABCC7 p.Arg104Glu 18449561:91:51
status: NEW92 b The degree of rectification in R104E, R117E, and K335E is dependent on the Cl-concentration.
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ABCC7 p.Arg104Glu 18449561:92:33
status: NEW104 In fact, at both sites, pCMBS had a greater effect on the rectification ratio than MTSES (P<0.05), making them closer to results obtained with R104E and R117E.
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ABCC7 p.Arg104Glu 18449561:104:143
status: NEW116 All mutants depicted (R104Q, R117Q, K335A, R104E, R117E, K335E) significantly different from wild type (asterisk P<0.05).
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ABCC7 p.Arg104Glu 18449561:116:43
status: NEW145 The reduction in unitary current for Cl-efflux seen in R104Q, R104E, and K335E (Fig. 4) further suggests that these residues may play an electrostatic role in Fig. 8 Mutation of positively charged residues weakens the apparent inhibitory effect of external Pt(NO2)4 2- ions.
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ABCC7 p.Arg104Glu 18449561:145:62
status: NEW
PMID: 25024266
[PubMed]
Cui G et al: "Three charged amino acids in extracellular loop 1 are involved in maintaining the outer pore architecture of CFTR."
No.
Sentence
Comment
117
Fig. S5 illustrates representative single-channel current traces of E116R/ K892E- and R104E/D110R-CFTR and their mean burst durations.
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ABCC7 p.Arg104Glu 25024266:117:86
status: NEW118 Fig. S6 shows representative I-V plots of double mutants R104E/ E116R- and R117E/E1126R-CFTR and their rectification ratio.
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ABCC7 p.Arg104Glu 25024266:118:57
status: NEW224 Tab l e 1 Reversal potentials of WT-CFTR and mutants in ND96 bath solution CFTR n Vrev mV WT 14 &#e032;27.75 &#b1; 0.78 R334A 6 &#e032;12.15 &#b1; 1.64a R117A 6 &#e032;22.51 &#b1; 0.85a E116R 5 &#e032;21.45 &#b1; 1.14a K114D 5 &#e032;24.68 &#b1; 3.22 D110R 5 &#e032;27.64 &#b1; 3.29 R104E 5 &#e032;21.15 &#b1; 1.08a R899C 4 &#e032;25.30 &#b1; 3.94 D891C 6 &#e032;25.81 &#b1; 2.44 K892E 5 &#e032;23.70 &#b1; 3.62 E1124R 5 &#e032;18.32 &#b1; 0.43a E1126R 5 &#e032;20.67 &#b1; 3.16b R117E/E1126R 6 &#e032;23.06 &#b1; 1.37b R104E/E116R 6 &#e032;27.17 &#b1; 1.08 Values are mean &#b1; SEM.
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ABCC7 p.Arg104Glu 25024266:224:283
status: NEWX
ABCC7 p.Arg104Glu 25024266:224:520
status: NEW233 E116 forms a salt bridge with R104 in the open state as well as in the closed state To test the above prediction that R104 is a partner for E116, we studied the single mutant R104E-CFTR and the charge-swap double mutants R104E/E116R- and R104E/D110R-CFTR.
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ABCC7 p.Arg104Glu 25024266:233:175
status: NEWX
ABCC7 p.Arg104Glu 25024266:233:221
status: NEWX
ABCC7 p.Arg104Glu 25024266:233:238
status: NEW235 Both R104E-CFTR and R104E/E116R-CFTR exhibited reduced outward rectification with similar reversal potentials, both significantly different from WT-CFTR (Figs.
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ABCC7 p.Arg104Glu 25024266:235:5
status: NEWX
ABCC7 p.Arg104Glu 25024266:235:20
status: NEW237 Single-channel recording of R104E-CFTR (representative trace in Fig. 9 A) revealed Instead, we found that mutations at E217, D891, R899, or E1124 had no significant effect on single-channel behavior (Fig. S4 A, bottom).
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ABCC7 p.Arg104Glu 25024266:237:28
status: NEW264 Mean burst duration of R104E-CFTR was 325 &#b1; 54.08 ms, significantly shorter than WT but significantly longer than E116R-CFTR (Fig. 9 A, right).
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ABCC7 p.Arg104Glu 25024266:264:23
status: NEW265 Single-channel behavior of the double mutant R104E/ E116R-CFTR was similar to R104E-CFTR, with a long, stable f open state and a mean burst duration significantly longer than that of E116R-CFTR (Fig. 9 A, right).
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ABCC7 p.Arg104Glu 25024266:265:45
status: NEWX
ABCC7 p.Arg104Glu 25024266:265:78
status: NEW267 In contrast, single-channel properties of the R104E/D110R-CFTR double mutant were not significantly different from the D110R-CFTR single mutant (Fig. S5), suggesting no interaction between R104 and D110.
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ABCC7 p.Arg104Glu 25024266:267:46
status: NEW284 (A) Representative single-channel current traces of R104E- and R104E/E116R-CFTR recorded with the same experimental conditions as Fig. 2 (left), their all-points amplitude histograms (middle), and mean burst durations (right).
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ABCC7 p.Arg104Glu 25024266:284:52
status: NEWX
ABCC7 p.Arg104Glu 25024266:284:63
status: NEW285 **, P < 0.01 indicates a significant difference between E116R- and R104E/ E116R-CFTR.
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ABCC7 p.Arg104Glu 25024266:285:67
status: NEW409 However, as noted previously for R104E/E116R-CFTR, the charge swap mutant did not completely recover the behavior of Figure 12.ߓ R117 forms a salt bridge with E1126 in the open state.
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ABCC7 p.Arg104Glu 25024266:409:33
status: NEW