ABCC7 p.Glu116Asp
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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."
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Sentence
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182
We generated D110E-, E116D-, and R117K-CFTR and observed their single-channel behavior with the inside-out patch technique in symmetrical 150 mM Cl&#e032; solution at VM = &#e032;100 mV.
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ABCC7 p.Glu116Asp 25024266:182:21
status: NEW185 Similar results were observed when the burst durations of E116D-CFTR and E116R-CFTR were compared (P < 0.001; Fig. 7, B and E).
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ABCC7 p.Glu116Asp 25024266:185:58
status: NEW218 D110, E116, and R117 do not interact with each other locally Because charge-retaining ECL1 amino acid mutations D110E, E116D, and R117K partially rescued a steady Figure 6.ߓ Some ECL1 mutants exhibit altered rectification.
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ABCC7 p.Glu116Asp 25024266:218:119
status: NEW246 (A-C) Representative single-channel currents of D110R- and D110E- (A), E116R- and E116D- (B), and R117A- and R117K-CFTR (C) recorded under the same conditions as Fig. 2 A.
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ABCC7 p.Glu116Asp 25024266:246:82
status: NEW248 (D) Mean single-channel amplitude of WT-, D110R-, D110E-, E116R-, E116D-, R117A-, and R117K-CFTR.
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ABCC7 p.Glu116Asp 25024266:248:66
status: NEW250 (E) Mean burst duration of WT-, D110R-, D110E-, E116R-, E116D-, R117A-, and R117K-CFTR.
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ABCC7 p.Glu116Asp 25024266:250:56
status: NEW251 #, P < 0.001 indicates differences between D110R- and D110E-CFTR or E116R- and E116D-CFTR; *, P < 0.05 indicates differences between R117A- and R117K-CFTR.
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ABCC7 p.Glu116Asp 25024266:251:79
status: NEW423 As shown here, mean burst durations of charge-retaining mutants D110E-, E116D-, and R117K-CFTR are significantly longer than their related charge-reversing or charge-destroying mutants D110R-, E116R-, and R117A-CFTR but distinctly shorter than that of WT-CFTR (Fig. 7).
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ABCC7 p.Glu116Asp 25024266:423:72
status: NEW