ABCC7 p.Ile1132Cys
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PMID: 19381710
[PubMed]
Fatehi M et al: "Novel residues lining the CFTR chloride channel pore identified by functional modification of introduced cysteines."
No.
Sentence
Comment
71
As described previously for modification of cysteines introduced into TM6 (Fatehi and Linsdell 2008) and the extracellular loop between TMs 1 and 2 (Zhou et al. 2008), MTSET and MTSES altered the IREL-V shape in S1118C, T1121C, T1122C, G1127C, V1129C, I1131C and I1132C.
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ABCC7 p.Ile1132Cys 19381710:71:263
status: NEW82 In contrast, I1131C and I1132C did not significantly affect the form of either the i-V relationship (Fig. 4b) or the I-V relationship (Fig. 3a).
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ABCC7 p.Ile1132Cys 19381710:82:24
status: NEW86 No changes in i-V shape were observed for I1131C or I1132C.
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ABCC7 p.Ile1132Cys 19381710:86:52
status: NEW91 Indeed, changes in unitary current amplitude were observed in S1118C, T1121C, T1122C, G1127C, V1129C, I1131C and I1132C, but not wild-type, when MTS reagents were included in the pipette solution (Fig. 6).
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ABCC7 p.Ile1132Cys 19381710:91:115
status: NEW119 In contrast, the other three mutations (V1129C, I1131C, I1132C) led to no change or even a slight increase in unitary current amplitude (Fig. 5b) and more minor effects of MTS modification, resulting in no change or a small decrease in amplitude with MTSES and increases in amplitude to levels above wild-type with MTSET (Fig. 9b).
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ABCC7 p.Ile1132Cys 19381710:119:56
status: NEW124 Under these conditions, SCN- block was significantly strengthened in I1132C (at hyperpolarized and depolarized voltages), S1118C (at hyperpolarized voltages), T1121C and V1129C (at depolarized voltages) and I1131C (at very depolarized voltages only) Fig. 4 Single-channel currents carried by cysteine mutant forms of CFTR.
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ABCC7 p.Ile1132Cys 19381710:124:69
status: NEW133 Under these conditions, SCN- permeability was significantly increased in S1118C and (to a lesser extent) T1122C and G1127C and unaltered in T1121C, V1129C, I1131C and I1132C (Fig. 11).
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ABCC7 p.Ile1132Cys 19381710:133:167
status: NEW161 a S1118C (d), T1121C (j), T1122C (), G1127C (h); b V1129C (m), I1131C (r), I1132C (.).
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ABCC7 p.Ile1132Cys 19381710:161:76
status: NEW187 * Significant difference from wild-type (P \ 0.05) I1131C, I1132C) represents mutations at the outermost mouth of the pore.
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ABCC7 p.Ile1132Cys 19381710:187:60
status: NEW191 Chloride conductance was further reduced by MTSES modification at these sites, indicating the detrimental effect of depositing a negative charge within the permeation pathway. Cysteine substitution at the outer mouth of the pore (V1129C, I1131C, I1132C) (Fig. 9b) had somewhat different effects.
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ABCC7 p.Ile1132Cys 19381710:191:246
status: NEW
PMID: 21796338
[PubMed]
Qian F et al: "Functional arrangement of the 12th transmembrane region in the CFTR chloride channel pore based on functional investigation of a cysteine-less CFTR variant."
No.
Sentence
Comment
90
A similar lack of effect following prolonged (>5 min) exposure to such high concentrations of both MTSES and MTSET was also observed in ten out of 19 cysteine-substituted mutants tested (I1131C, I1132C, L1133C, T1134C, L1135C, A1136C, M1137C, I1139C, L1143C, and A1146C).
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ABCC7 p.Ile1132Cys 21796338:90:195
status: NEW126 Previous work from our group suggested that externally applied MTS reagents could modify cysteines only in the outermost part of TM12, namely, I1131C and I1132C [11]; these same cysteines were insensitive to internally applied MTS reagents (Fig. 2), again consistent with impermeability to these reagents.
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ABCC7 p.Ile1132Cys 21796338:126:154
status: NEW