ABCMdb

ABCC7 p.Asp58Ala

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Publications

PMID: 11468285 [PubMed] Fu J et al: "Cysteine substitutions reveal dual functions of the amino-terminal tail in cystic fibrosis transmembrane conductance regulator channel gating."

No. Sentence Comment

4 The MTS reagents had negligible effects on the gating of the wild type channel or a corresponding double alanine mutant (E54A/D58A) under the same conditions. Login to comment
40 This inhibition of opening rate was observed at concentrations of MTS reagents that had no effect on the gating of the wild type channel or of a corresponding alanine mutant (E54A/D58A). Login to comment
89 In addition, like the corresponding double alanine mutant (E54A/D58A) (13), the double cysteine mutant deactivated faster than wild type CFTR fol- lowing removal of the cAMP-activating mixture (Fig. 1C). Login to comment
96 We also tested the effects of MMTS on the wild type channel (WT CFTR) and the double alanine mutant (E54A/D58A) to determine if the inhibition was specifically due to modification of the engineered cysteines at residues 54 and 58. Login to comment
97 At this concentration MMTS had small effects (5-10% inhibition) on the macroscopic currents mediated by WT CFTR and E54A/ D58A in intact oocytes (Fig. 2, A and B) and had no effects on the channel activities of these constructs in excised patches (see below). Login to comment
108 When added to the cytoplasmic face of excised patches, MMTS had little effect on the channel open probability and gating kinetics (opening rate, burst duration) of either wild type CFTR or the double alanine mutant (E54A/D58A) (Fig. 3, A and B). Login to comment
138 More cRNA was injected for the mutants than for WT CFTR to achieve approximately the same absolute current levels following activation with the cAMP mixture (2 ng for E54C/D58C; 1 ng for E54C and E54A/D58A, and 0.5 ng for WT CFTR). Login to comment
143 A and B, representative channel records showing negligible effects of 10 ␮M MMTS on the gating of WT CFTR and E54A/D58A CFTR. Login to comment
212 This inhibitory effect was not observed for the wild type channel or for a corresponding double alanine mutant (E54A/D58A), which argues against a nonspecific effect of these reagents on channel activity. Login to comment

PMID: 11600681 [PubMed] Fu J et al: "A cluster of negative charges at the amino terminal tail of CFTR regulates ATP-dependent channel gating."

No. Sentence Comment

18 Replacing this and two nearby acidic residues with alanines (D47A, E54A, D58A) also reduced channel activity, but had negligible effects on bulk PKA phosphorylation or on the ATP dependence of channel activation. Login to comment
58 The N-tail triple mutant (D47A, E54A, D58A) was prepared by using the Stratagene site-directed mutagenesis kit. Login to comment
113 The currents mediated by D58N CFTR were somewhat greater than CFTR channel regulation by the amino tailJ. Physiol. 536.2 those observed for a triple mutant in which three acidic residues were replaced with alanines (D47A, E54A, D58A). Login to comment
119 D58N CFTR and N-tail triple mutant (D47A, E54A, D58A) exhibit lower macroscopic currents and faster deactivation than wild-type CFTR A, schematic diagram of CFTR topology (left) and helical wheel plot of N-tail region of interest (right) showing locations of the mutations analysed in this study. Login to comment
167 The N-tail mutations have little effect on bulk CFTR phosphorylation A, in vitro phosphorylation of wild-type (WT) CFTR and double (E54A, D58A) and triple N-tail mutants. Login to comment
228 To further examine the mechanism by which the N-tail modulates ATP-dependent channel gating, we tested the responses of the wild-type and N-tail triple mutant (D47A, E54A, D58A) to ATP and AMP-PNP in single channel studies. Login to comment