ABCC7 p.Ser623Ala
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PMID: 20435887
[PubMed]
Billet A et al: "C terminus of nucleotide binding domain 1 contains critical features for cystic fibrosis transmembrane conductance regulator trafficking and activation."
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2
We mutated CFTR amino acids located in the betac5-betac6 hairpin, within the betac5 strand (H620Q), within the beta-turn linking the two beta strands (E621G, G622D), as well as within (S623A, S624A) and at the extremity (G628R) of the betac6 strand.
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ABCC7 p.Ser623Ala 20435887:2:185
status: NEW3 Functional analysis reveals that the current density was largely reduced for G622D and G628R channels compared with wt CFTR, similar for E621G and S624A, but increased for H620Q and S623A.
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ABCC7 p.Ser623Ala 20435887:3:182
status: NEW5 In addition, in presence of the CFTR activator benzo[c]quinolizinium, the CFTR current density compared with that of wt CFTR was abolished for G622D and G628R channels, but similar for H620Q, S623A, and S624A or slightly increased for E621G.
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ABCC7 p.Ser623Ala 20435887:5:192
status: NEW33 We have mutated these two glycine residues in aspartic acid (G622D) and arginine (G628R) and considered other mutants in their neighborhood (H620Q, E621G, S623A, and S624A).
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ABCC7 p.Ser623Ala 20435887:33:155
status: NEW87 RESULTS Expression of the NBD1 C-terminal CFTR Mutants-We have introduced EGFP-tagged CFTR proteins into HEK293 cells, wt CFTR and six CFTR mutants, i.e. H620Q, E621G, G622D, S623A, S624A, and G628R.
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ABCC7 p.Ser623Ala 20435887:87:175
status: NEW90 For the expression of CFTR mutants H620Q, E621G, S623A, and S624A, the profiles of core-glycosylated and mature-glycosylated forms were similar to that of the wt protein.
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ABCC7 p.Ser623Ala 20435887:90:49
status: NEW109 Second, with the two mutations introduced on both sides of the beta turn, H620Q and S623A, we recorded an increased (p Ͻ 0.001) Cl- current (supplemental Table 2) compared with wt CFTR.
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ABCC7 p.Ser623Ala 20435887:109:84
status: NEW122 Concerning the activation kinetics, only the two CFTR mutants with an increased Cl-transport activity (H620Q and S623A) also present a faster time course of activation (Fig. 5B).
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ABCC7 p.Ser623Ala 20435887:122:113
status: NEW124 T50 of the two mutated channels (T50 ϭ 124.45 Ϯ 8.8 s for H620Q, n ϭ 8 and T50 ϭ 114.63 Ϯ 8.8 s for S623A, n ϭ 8) were significantly different compared with wt (T50 ϭ 164.85 Ϯ 10.2 s, n ϭ 8).
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ABCC7 p.Ser623Ala 20435887:124:130
status: NEW125 Our results indicated that H620Q and S623A channels could be activated more rapidly than the other CFTR mutant channels studied.
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ABCC7 p.Ser623Ala 20435887:125:37
status: NEW130 Interestingly, although the level of current for H620Q and S623A was greater than the response of wt channels (Fig. 3), both mutated CFTRs were activated by MPB-91 to a level similar to that of wt CFTR (Fig. 6) (at 40 mV, current densities were: H620Q, 27.86 Ϯ 4.2 pA/pF, n ϭ 5; S623A, 30.83 Ϯ 3.4 pA/pF, n ϭ 6).
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ABCC7 p.Ser623Ala 20435887:130:59
status: NEWX
ABCC7 p.Ser623Ala 20435887:130:291
status: NEW138 Dotted line corresponds to the wt level. B, upper, representatives time course of wt and S623A mutant in the presence of 10 M Fsk.
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ABCC7 p.Ser623Ala 20435887:138:89
status: NEW163 In particular, the cAMP-activated Cl- current densities elicited by H620Q and S623A channels were increased compared with wt.
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ABCC7 p.Ser623Ala 20435887:163:78
status: NEW176 Dotted line corresponds to the wt level. B, upper, representatives time course of wt and S623A mutant in presence of 50 M MPB-91.
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ABCC7 p.Ser623Ala 20435887:176:89
status: NEW180 In addition, MPB-91 was also able to activate H620Q, E621G, S623A, and S624A mutants.
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ABCC7 p.Ser623Ala 20435887:180:60
status: NEW182 Contrary to the activation by Fsk, no difference of kinetic parameters was detected with the two mutants H620Q and S623A.
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ABCC7 p.Ser623Ala 20435887:182:115
status: NEW