ABCC7 p.Arg764Ala

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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."
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11 First, not only D835A, D836A and E838A but also K946A reduced the PKA dependent CFTR activation.
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ABCC7 p.Arg764Ala 23060444:11:7
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13 Third, R764A and R766A mutants enhanced the PKA-dependent activation.
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ABCC7 p.Arg764Ala 23060444:13:7
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116 The effects of R764A and R766A on the PKA-dependent channel activation - Because both S768 and D836 are close to H950 of CL3, it is fitting to ask if R764, R765 and R766 form a salt bridge with the N-terminal of NEG2 to cause the asymmetry of the electrostatic regulation.
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ABCC7 p.Arg764Ala 23060444:116:15
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118 Fig. 4D demonstrates that both R764A and R766A exhibited a normal channel density.
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ABCC7 p.Arg764Ala 23060444:118:31
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121 The K1/2 for PKA activation of R764A and R766A increased from 10 units/ml to 25 and 44 units/ml, respectively.
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ABCC7 p.Arg764Ala 23060444:121:31
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140 Finally, it is very exciting that the putative electrostatic attraction between K946D/H950D and D835R/D836R/E838R dramatically suppressed the channel activity by stopping the channel processing or opening(10).
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ABCC7 p.Arg764Ala 23060444:140:15
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145 Our finding shows that R764A and R766A suppressed not the channel processing and the current density but the channel activation by PKA (Fig. 4-6).
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ABCC7 p.Arg764Ala 23060444:145:23
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142 Fig. 4D demonstrates that both R764A and R766A exhibited a normal channel density.
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ABCC7 p.Arg764Ala 23060444:142:31
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151 The currents mediated by S768D/K946D/H950D/D836R and S768D/K946D/H950D/E838R were statistically smaller than the S768D/K946D/H950D current (n afd; 3,*, p b0d; 0.05, unpaired t test); error bars, S.E. TABLE 1 WholecellcurrentsIm (picoamperes)andcapacitancesCm (picofarads) of HEK-293T cells expressing CFTR constructs in response to forskolin Constructs Stimulated Im Control Cm Stimulated Cm n WT-CFTR 701.6 afe; 9.0 17.4 afe; 0.9 16.4 afe; 1.1 3 D835R/D836R/E838R 539.5 afe; 5.3 15.0 afe; 1.0 16.2 afe; 0.8 3 Asymmetric Electrostatic Regulation of CFTR 40488 JOURNAL OF BIOLOGICAL CHEMISTRY VOLUME 287ߦNUMBER 48ߦNOVEMBER 23, 2012 at SEMMELWEIS UNIV OF MEDICINE on December , The K1/2 for PKA activation of R764A and R766A increased from 10 units/ml to 25 and 44 units/ml, respectively.
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ABCC7 p.Arg764Ala 23060444:151:744
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173 The PKA-dependent activity of CFTR mutants R764A and R766A.
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ABCC7 p.Arg764Ala 23060444:173:43
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179 B, PKA titration curves for CFTR mutants R764A and R766A (n afd; 3-5).
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ABCC7 p.Arg764Ala 23060444:179:41
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184 Our finding shows that R764A and R766A suppressed not the channel processing and the current density but the channel activation by PKA (Figs. 4-6).
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ABCC7 p.Arg764Ala 23060444:184:23
status: NEW
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