ABCC7 p.Arg117Glu

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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.Arg117Glu 18449561:60:100
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67 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.Arg117Glu 18449561:67:120
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73 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.Arg117Glu 18449561:73:118
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79 However, current amplitude was significantly reduced in R104E, R117E, and K335E (Fig. 4a, b).
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ABCC7 p.Arg117Glu 18449561:79:63
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91 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.Arg117Glu 18449561:91:58
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92 b The degree of rectification in R104E, R117E, and K335E is dependent on the Cl-concentration.
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ABCC7 p.Arg117Glu 18449561:92:40
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95 Mean of data from four to six patches in both a and b side chains bearing different charges (Fig. 5b), with the possible exception that R117C modified by MTSES did not show the same degree of inward rectification seen in R117E.
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ABCC7 p.Arg117Glu 18449561:95:223
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104 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.Arg117Glu 18449561:104:153
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116 All mutants depicted (R104Q, R117Q, K335A, R104E, R117E, K335E) significantly different from wild type (asterisk P<0.05).
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ABCC7 p.Arg117Glu 18449561:116:50
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137 The charge on the side chain is assumed to be +1 (MTSET, WT), 0 (R104/ 117C, R104/117Q), or -1 (MTSES, R104/R117E).
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ABCC7 p.Arg117Glu 18449561:137:108
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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
118 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.Arg117Glu 25024266:118:75
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128 No current was detected in either inside-out patch or TEVC recording from oocytes expressing R117E-CFTR; therefore, it was not studied further.
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ABCC7 p.Arg117Glu 25024266:128:93
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204 To test this hypothesis, we first made the mutants E116R/R117E-, D110R/R117E-, and D110R/E116R/R117E-CFTR and studied their single-channel properties.
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ABCC7 p.Arg117Glu 25024266:204:57
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ABCC7 p.Arg117Glu 25024266:204:71
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ABCC7 p.Arg117Glu 25024266:204:95
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224 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.Arg117Glu 25024266:224:480
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271 (A) Representative single-channel currents of R117E/ E116R-, R117E/D110R-, and R117E/E116R/ D110R-CFTR and corresponding all-points amplitude histograms recorded under the same conditions as Fig. 2 A.
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ABCC7 p.Arg117Glu 25024266:271:46
status: NEW
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ABCC7 p.Arg117Glu 25024266:271:61
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ABCC7 p.Arg117Glu 25024266:271:79
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274 (C) Mean single-channel amplitudes of WT-, R117E/ E116R-, R117E/D110R-, and R117E/E116R/ D110R-CFTR.
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ABCC7 p.Arg117Glu 25024266:274:43
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ABCC7 p.Arg117Glu 25024266:274:58
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ABCC7 p.Arg117Glu 25024266:274:76
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380 Sample current traces for both E1126R- and R117E/ E1126R-CFTR are shown in Fig. 12 A.
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ABCC7 p.Arg117Glu 25024266:380:43
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381 As mentioned previously, we did not detect current from R117E-CFTR We also tested the possibility that E116 could form an open state salt bridge with K892.
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ABCC7 p.Arg117Glu 25024266:381:56
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403 We also compared the fractional burst duration represented by s1, s2, and f states for E1126R- and R117E/E1126R-CFTR and found that E1126R exhibited a significantly higher fraction of both s1 and s2 states than WT, whereas the distribution for double mutant R117E/E1126R-CFTR was similar to WT-CFTR, exhibiting mainly the f state (a nearly complete rescue; Fig. 12 D).
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ABCC7 p.Arg117Glu 25024266:403:99
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ABCC7 p.Arg117Glu 25024266:403:258
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406 R117E/E1126R-CFTR opened to a full open state much more often compared with R117A-CFTR (Fig. 2).
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ABCC7 p.Arg117Glu 25024266:406:0
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407 Mean burst duration for both E1126R- and R117E/ E1126R-CFTR are summarized in Fig. 12 B.
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ABCC7 p.Arg117Glu 25024266:407:41
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408 The mean burst duration of R117E/E1126R-CFTR was significantly longer than that of R117A- and R117C-CFTR.
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ABCC7 p.Arg117Glu 25024266:408:27
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410 (A) Representative single-channel current traces of E1126R-, R117E/E1126R-, R117C-, and R117C/E1126C-CFTR recorded under the same experimental conditions as Fig. 2 and their all-points amplitude histograms (right).
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ABCC7 p.Arg117Glu 25024266:410:61
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412 #, P < 0.01 indicates a significant difference between WTand R117C-CFTR; **, P < 0.01 indicates a significant difference between WTand E1126R-CFTR, between R117C and R117E/E1126R-CFTR, and between R117C and R117C/E1126C.
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ABCC7 p.Arg117Glu 25024266:412:166
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413 n.d., no current detected for R117E-CFTR in Xenopus oocytes.
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ABCC7 p.Arg117Glu 25024266:413:30
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417 (D) Mean fraction of open burst duration is plotted for each open conductance state of E1126R- and R117E/E1126R-CFTR.
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ABCC7 p.Arg117Glu 25024266:417:99
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