ABCC7 p.Asn1148Cys
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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
62
b Example leak subtracted I-V relationships for N1138C, T1142C, V1147C, and N1148C, recorded from inside out membrane patches following maximal channel activation with PKA, ATP, and PPi.
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ABCC7 p.Asn1148Cys 21796338:62:76
status: NEW64 As described in the text, whereas MTSES application always led to a decrease in macroscopic current amplitude in reactive mutants, the effects of MTSET were to decrease (e.g., N1138C, V1147C), increase (e.g., T1142C) or not significantly alter (e.g., N1148C) macroscopic current amplitude.
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ABCC7 p.Asn1148Cys 21796338:64:251
status: NEW80 Application of MTSES (200 μM) or MTSET (2 mM) to the intracellular solution after channel activation with PKA, ATP, and PPi significantly altered macroscopic current amplitude in nine out of 19 cysteine-substituted mutants tested (N1138C, M1140C, S1141C, T1142C, Q1144C, W1145C, V1147C, N1148C, and S1149C; Figs. 1 and 2).
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ABCC7 p.Asn1148Cys 21796338:80:293
status: NEW86 However, unlike previous findings in TM6 [9], we observed a third pattern for cysteines introduced closest to the putative cytoplasmic end of TM12 (V1147C, N1148C, and S1149C).
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ABCC7 p.Asn1148Cys 21796338:86:156
status: NEW87 Here, macroscopic current amplitude was decreased by MTSES application but either decreased (V1147C, S1149C) or not significantly affected (N1148C) by MTSET application.
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ABCC7 p.Asn1148Cys 21796338:87:140
status: NEW
PMID: 22042986
[PubMed]
Bai Y et al: "Structural basis for the channel function of a degraded ABC transporter, CFTR (ABCC7)."
No.
Sentence
Comment
154
(A and B) Single-channel recordings at 50 mV show that application of MTSET+ increases unitary current amplitudes for cysless/N1148C (A) or cysless/W1145C (B).
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ABCC7 p.Asn1148Cys 22042986:154:134
status: NEW155 Linear fits to single-channel current measurements at different voltages yield unitary conductance values for cysless/ N1148C (A) of 7.1 pS before (black) and 9.2 pS after (blue) MTSET+ treatment, for cysless/W1145C (B) of 7.6 pS before (black) and 10.1 pS after (blue) MTSET+ treatment.
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ABCC7 p.Asn1148Cys 22042986:155:119
status: NEW180 Note that the modification is faster in the presence of ATP than in the absence of ATP for cysless/N1148C-CFTR channels (B), whereas it is slower in the presence of ATP than in the absence of ATP for cysless/S1141C-CFTR channels (C).
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ABCC7 p.Asn1148Cys 22042986:180:99
status: NEW198 (C) Second-order rate constants (MTSES ) of Texas red MTSEA+ modification for cysless/ S1141C-, cysless/N1148C-, cysless/ I344C-, and cysless/M348C-CFTR channels.
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ABCC7 p.Asn1148Cys 22042986:198:121
status: NEW
PMID: 25143385
[PubMed]
El Hiani Y et al: "Metal bridges illuminate transmembrane domain movements during gating of the cystic fibrosis transmembrane conductance regulator chloride channel."
No.
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Comment
51
To investigate potential Cd2af9; bridges formed between pore-lining cysteine side chains exposed in the inner vestibule of the CFTR pore, we combined individual cysteines that we previously found to be accessible to cytoplasmically applied methanethiosulfonate reagents in three important pore-lining TMs: TM1 (K95C, Q98C) (13), TM6 (I344C, V345C, M348C, A349C) (15), and TM12 (M1140C, S1141C, T1142C, Q1144C, W1145C, V1147C, N1148C) (16), to generate a total of 50 double cysteine mutants (8 TM1:TM6; 14 TM1:TM12; 28 TM6:TM12).
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ABCC7 p.Asn1148Cys 25143385:51:429
status: NEW71 In contrast, the remaining seven double cysteine mutants, namely I344C/S1141C (Fig. 2, C and D), V345C/S1141C, M348C/ S1141C (Fig. 2, C and E), M348C/V1144C, M348C/W1145C, M348C/V1147C, and M348C/N1148C, all showed increased sensitivity to Cd2af9; , leading to a significant decrease in Ki as compared with either of the single cysteine mutants from which they were derived (estimated Ki values b0d; 50 òe;M; Fig. 3).
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ABCC7 p.Asn1148Cys 25143385:71:196
status: NEW137 Thus, M348C is able to form Cd2af9; bridges with cysteines at multiple positions in TM12 (S1141C, Q1144C, W1145C, V1147C, N1148C) (Fig. 8B), and S1141C is able to form Cd2af9; bridges with cysteines both in TM1 (K95C) and in TM6 (I344C, V345C, M348C) (Fig. 8C).
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ABCC7 p.Asn1148Cys 25143385:137:125
status: NEW
No.
Sentence
Comment
192
[Au(CN)2]- , forskolin, with G1349D, /M/s Outside R334C 189 &#b1; 39 - 403 &#b1; 20 537 &#b1; 56 K335C - - 56 &#b1; 9 1,809 &#b1; 201 F337C 437 &#b1; 49 - 20 &#b1; 3 32 &#b1; 6 T338C 752 &#b1; 59 - 1,135 &#b1; 166 118 &#b1; 18 Inside I344C 32 &#b1; 5 37 &#b1; 4 - - N1148C 437 &#b1; 66 2,089 &#b1; 130 - - Residues located extracellularly (extra.)
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ABCC7 p.Asn1148Cys 25675504:192:266
status: NEW