ABCMdb

ABCC7 p.Ala462Phe

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Publications

PMID: 15623556 [PubMed] Berger AL et al: "Normal gating of CFTR requires ATP binding to both nucleotide-binding domains and hydrolysis at the second nucleotide-binding domain."

No. Sentence Comment

71 The 6% gels revealed that CFTR-A462F and -K464A produced little band C protein, whereas other variants produced predominantly the band C form. Login to comment
103 The A462F mutation prevented labeling of NBD1; S1248F blocked NBD2 labeling; and the double mutant A462F͞S1248F abolished labeling at both NBDs. Login to comment
154 To assess the gating effects of ATP binding to NBD1, we studied the A462F variant, which blocks NBD1 nucleotide binding. Login to comment
156 A462F reduced Po, as did treating A462C channels with NEM. Login to comment
179 (A) Examples of recordings from CFTR-A462F, and of A462C channels before and after NEM treatment. Login to comment
180 Although the A462F tracing shown has a higher Po than the mean, we chose this example to show the bursts. Login to comment
250 However, that is not what we observed; the A462F mutation completely blocked NBD1 labeling, and S1248F blocked NBD2 labeling. Login to comment
253 Nevertheless, we did find that the A462F mutation in NBD1 diminished labeling of NBD2 and that S1248F slightly reduced NBD1 labeling. Login to comment

PMID: 17178710 [PubMed] Wang W et al: "Curcumin opens cystic fibrosis transmembrane conductance regulator channels by a novel mechanism that requires neither ATP binding nor dimerization of the nucleotide-binding domains."

No. Sentence Comment

174 Fig. 4 (D and E) shows that the inhibitory effect of bath ATP on the curcumin response was eliminated by introducing a mutation in the Walker A sequence (A462F) in NBD1. Login to comment
176 The lack of effect of ATP on the curcumin activation of the A462F/⌬1198-CFTR construct FIGURE 3. Login to comment
195 D, bath ATP does not inhibit A462F/⌬1198-CFTR channels. Login to comment
196 E, mean data comparing the effects of bath ATP (1.5 mM) on ⌬1198-CFTR (n ϭ 16) and A462F/⌬1198-CFTR (n ϭ 10) activation by 30 ␮M curcumin. Login to comment
198 Note that the absolute currents mediated by A462F/⌬1198-CFTR are lower because the A462F mutation partially disrupts ER processing and cell surface localization (33).3 All of the records are representative of at least three experiments. Login to comment
246 Introducing a mutation in the Walker A motif that was shown previously to disrupt ATP binding to NBD1 (A462F (33)) severely blunted the inhibitory effect of ATP on ⌬1198-CFTR channel activation by curcumin. Login to comment

PMID: 21059651 [PubMed] Wang G et al: "The inhibition mechanism of non-phosphorylated Ser768 in the regulatory domain of cystic fibrosis transmembrane conductance regulator."

No. Sentence Comment

268 Role of Curcumin in Normal CFTR Gating-A previous study (21) showed that curcumin activates mutant CFTR channels, such as G551D, W1282X, ⌬1198, and A462F. Login to comment

PMID: 21419343 [PubMed] Khushoo A et al: "Ligand-driven vectorial folding of ribosome-bound human CFTR NBD1."

No. Sentence Comment

114 In addition, mutations that inhibit ATP binding to NBD1 in full-length CFTR (W401A, A462F, and K464A [Berger et al., 2005]) also inhibited binding to truncated NBD1 (Figures 5E and 5F). Login to comment
205 The CFP-NBD1 ATP-binding mutant contained W401A, A462F, and K464A mutations in the ATP-binding site as predicted by the crystal structure (2BBO). Login to comment

PMID: 22948143 [PubMed] Randak CO et al: "Demonstration of Phosphoryl Group Transfer Indicates That the ATP-binding Cassette (ABC) Transporter Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Exhibits Adenylate Kinase Activity."

No. Sentence Comment

165 We could not assess the effect of the homologous mutation in ATP-binding site 1 (A462F mutation) on adenylate kinase activity because that mutation affected intracellular CFTR processing to an extent that we were unable to detect the mutant CFTR protein in our membrane preparations by Western blot. Login to comment
164 We could not assess the effect of the homologous mutation in ATP-binding site 1 (A462F mutation) on adenylate kinase activity because that mutation affected intracellular CFTR processing to an extent that we were unable to detect the mutant CFTR protein in our membrane preparations by Western blot. Login to comment

PMID: 23921386 [PubMed] Randak CO et al: "ATP and AMP mutually influence their interaction with the ATP-binding cassette (ABC) adenylate kinase cystic fibrosis transmembrane conductance regulator (CFTR) at separate binding sites."

No. Sentence Comment

94 Recordings from patches containing very few channels (A462F CFTR) with up to five simultaneous channel openings were low pass-filtered at 500 Hz for analysis. Login to comment
238 Berger et al. (15) found that substituting alanine at position 462 in NBD1 with phenylalanine (A462F mutation; Fig. 9B, left) abolished nucleotide interaction with ATP-binding site 1. Login to comment
241 The A462F, but not the S1248F mutation interfered with processing and trafficking to the cell membrane (supplemental Fig. S1), and hence, the number of channels in excised membrane patches was small; therefore, we quantified channel activity as NPo. Login to comment
242 We found that Ap5A reduced the NPo of A462F CFTR (Fig. 9B, middle and right). Login to comment
261 B, left, model of A462F CFTR. Login to comment
262 Middle, current recording from one excised inside-out membrane patch containing at least two A462F CFTR channels perfused on cytosolic surface with ATP and Ap5A as indicated. Login to comment
268 Right, NPo of A462F CFTR with 0.3 mM ATP and PKA present in the bath solution before and after adding 1 mM Ap5A. Login to comment