ABCC7 p.Gln493Ala
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PMID: 16442101
[PubMed]
Frelet A et al: "Insight in eukaryotic ABC transporter function by mutation analysis."
No.
Sentence
Comment
299
[137] Q493A, Q1291A, N505C, N1303K Q493A and N505C reduced and increased the frequency of CO, respectively.
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ABCC7 p.Gln493Ala 16442101:299:6
status: NEWX
ABCC7 p.Gln493Ala 16442101:299:35
status: NEW
PMID: 11788611
[PubMed]
Berger AL et al: "Mutations that change the position of the putative gamma-phosphate linker in the nucleotide binding domains of CFTR alter channel gating."
No.
Sentence
Comment
4
In NBD1, Q493A reduced the frequency of channel opening, suggesting a role for this residue in coupling ATP binding to channel opening.
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ABCC7 p.Gln493Ala 11788611:4:9
status: NEW79 Single-channel gating of wild type CFTR, CFTR-Q493A, and CFTR-Q1291A.
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ABCC7 p.Gln493Ala 11788611:79:46
status: NEW80 A, examples of current from excised inside-out membrane patches containing single CFTR channels in the presence of 1 mM ATP and 75 nM PKA. Membrane potential was clamped at -80 mV. B, data from multiple patches. Asterisk indicates p Ͻ 0.05; n ϭ 7 for WT, n ϭ 4 for CFTR-Q493A, and n ϭ 3 for CFTR-Q1291A.
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ABCC7 p.Gln493Ala 11788611:80:288
status: NEW93 In contrast, the Q493A variant exhibited a substantially reduced Po because of a prolonged interburst interval with little change in FIG. 3.
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ABCC7 p.Gln493Ala 11788611:93:17
status: NEW94 Wild type CFTR, CFTR-Q493A, and CFTR-Q1291A had similar dose response curves for ATP-stimulated Cl- current.
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ABCC7 p.Gln493Ala 11788611:94:21
status: NEW98 The apparent EC50 was 176 Ϯ 67 M for wild type CFTR, 217 Ϯ 55 M for CFTR-Q493A, and 159 Ϯ 70 M for CFTR-Q1291A.
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ABCC7 p.Gln493Ala 11788611:98:101
status: NEW101 Wild type CFTR, CFTR-Q493A, and CFTR-Q1291A showed similar cation requirements for Cl-channel activity.
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ABCC7 p.Gln493Ala 11788611:101:21
status: NEW112 Because ATP binding may open the CFTR Cl-channel (13, 14), thereby reducing the interburst interval, we asked if the prolonged interburst interval in Q493A was consistent with attenuated binding.
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ABCC7 p.Gln493Ala 11788611:112:150
status: NEW114 Wild type CFTR and CFTR-Q493A had the same apparent EC50 for ATP (Fig. 3).
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ABCC7 p.Gln493Ala 11788611:114:24
status: NEW121 Wild type CFTR, CFTR-Q493A, and CFTR-Q1291A were all inhibited by ADP.
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ABCC7 p.Gln493Ala 11788611:121:21
status: NEW122 A, examples of patches incubated with ATP (1 mM) and ADP (1 mM) during the times indicated. B, data from multiple patches show that wild type CFTR, CFTR-Q493A, and CFTR-Q1291A currents were inhibited by ADP to a similar extent.
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ABCC7 p.Gln493Ala 11788611:122:153
status: NEW127 The membrane potential was clamped at -40 mV. Patches were incubated with 1 mM ATP and 4 mM PPi during the times indicated. B, data from multiple patches show that 4 mM PPi stimulated less Cl- current in CFTR-Q1291A (n ϭ 6) than in wild type CFTR (n ϭ 4) or CFTR-Q493A (n ϭ 4).
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ABCC7 p.Gln493Ala 11788611:127:275
status: NEW130 Fig. 4 shows that varying the divalent cation generated similar effects for wild type CFTR and the Q493A variant.
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ABCC7 p.Gln493Ala 11788611:130:99
status: NEW134 The Q493A mutation did not alter the response to either agent (Figs.
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ABCC7 p.Gln493Ala 11788611:134:4
status: NEW136 Mutating Asn-505 in NBD1 Can Increase Channel Opening-The N505C mutation had an effect opposite to that of Q493A; it reduced the interburst interval and increased Po (Fig. 7).
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ABCC7 p.Gln493Ala 11788611:136:107
status: NEW137 As with Q493A, burst duration did not change.
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ABCC7 p.Gln493Ala 11788611:137:8
status: NEW141 The opposite effects of the Q493A and N505C mutations on gating are consistent with the expectation that these mutations might have different effects on the ␥-phosphate linker.
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ABCC7 p.Gln493Ala 11788611:141:28
status: NEW