ABCC7 p.Lys946Ala
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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
141
Similarly, curcumin also activated mutants K946A, K951A, S955A, and Q958A to a different extent in the presence of ATP (Fig. 4E).
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ABCC7 p.Lys946Ala 21059651:141:43
status: NEW234 Error bars, S.E. TABLE 1 Potential roles in hydrogen bonding at the CL3-R domain interface Note that mutants whose channel activity was increased by curcumin in the presence of ATP are highlighted in boldface type. Residues Role in H-bond Mutants Arg Strong donor H950R, S768R, H950R/S768R, H950R/S768D, H950D/S768R Asp Strong acceptor H950D, S768D, H950D/S768D, H950R/S768D, H950D/S768R Thr, Gln, Ser, His Donor/Acceptor H950Q, S768T, WT Ala Negative control K946A, H950A, K951A, H954A, S955A, Q958A, S737A, S768A, ⌬R Inhibition of CFTR by Ser768 JANUARY 21, 2011•VOLUME 286•NUMBER 3 JOURNAL OF BIOLOGICAL CHEMISTRY 2177 matter whether cAMP was present or not in the extracellular perfusate.
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ABCC7 p.Lys946Ala 21059651:234:460
status: NEW314 On the other hand, K946A, K951A, S955A, and Q958A still promoted channel opening by ATP followed by curcumin (Fig. 4, E and F).
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ABCC7 p.Lys946Ala 21059651:314:19
status: NEW
PMID: 23060444
[PubMed]
Wang G et al: "Regulation of Activation and Processing of the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) by a Complex Electrostatic Interaction between the Regulatory Domain and Cytoplasmic Loop 3."
No.
Sentence
Comment
11
First, not only D835A, D836A and E838A but also K946A reduced the PKA dependent CFTR activation.
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ABCC7 p.Lys946Ala 23060444:11:48
status: NEW64 In the presence of 1.5mM ATP, 50µM curcumin greatly potentiated the K946A mutant activity, which was further increased by PKA (Fig. 3A).
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ABCC7 p.Lys946Ala 23060444:64:73
status: NEW138 First, the PKA sensitivity of channel activation was significantly enhanced for K946A, D835A, D836A and E838A mutants (Fig.2).
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ABCC7 p.Lys946Ala 23060444:138:80
status: NEW139 Second, the curcumin sensitivity was also increased for K946A, K946D and D835R/D836R/E838R (Fig.3).
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ABCC7 p.Lys946Ala 23060444:139:56
status: NEW9 First, not only D835A, D836A, and E838A but also K946A reduced the PKA-dependent CFTR activation.
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ABCC7 p.Lys946Ala 23060444:9:49
status: NEW62 In contrast, mutation of Lys-946 or Asp-836 to alanine clearly accelerated the channel activation and reduced the PKA dependence (Fig. 2, B and C).
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ABCC7 p.Lys946Ala 23060444:62:25
status: NEW68 In the presence of 1.5 mM ATP, 50 òe;M curcumin greatly potentiated the K946A mutant activity, which was further increased by PKA (Fig. 3A).
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ABCC7 p.Lys946Ala 23060444:68:76
status: NEW98 The PKA-dependent activity of CFTR mutants at the R-CL3 interface. A-C, macroscopic currents across inside-out membrane patches excised from transfected HEK-293T cells expressing WT CFTR (A) and mutants K946A (B) and D836A (C) by using a ramp protocol (afe;80 mV).
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ABCC7 p.Lys946Ala 23060444:98:203
status: NEW127 Macroscopic currents across inside-out membrane patches excised from transfected HEK-293T cells expressing CFTR mutants K946A (A), K946D (B) and D835R/D836R/E838R (C) by using a ramp protocol (afe;80 mV) are shown.
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ABCC7 p.Lys946Ala 23060444:127:120
status: NEW167 First, the PKA sensitivity of channel activation was significantly enhanced for K946A, D835A, D836A, and E838A mutants (Fig. 2).
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ABCC7 p.Lys946Ala 23060444:167:80
status: NEW168 Second, the curcumin sensitivity was also increased for K946A, K946D, and D835R/ D836R/E838R (Fig. 3).
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ABCC7 p.Lys946Ala 23060444:168:56
status: NEW