ABCC7 p.Ser790Ala

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PMID: 11331356 [PubMed] Button B et al: "PKC-mediated stimulation of amphibian CFTR depends on a single phosphorylation consensus site. insertion of this site confers PKC sensitivity to human CFTR."
No. Sentence Comment
73 plus addition of HaeIII site), 5Ј-GTCAAGAATAAAGCTTTTAAG- CAGG-3Ј (Ser686 to Ala, plus addition of HindIII site), 5Ј-TGGG- GATTTCGCTGAGAAAAGAAAGAG-3Ј (Ser694 to Ala, plus addition of DdeI site), and 5Ј-CAAGAAAAACTGCAGTTCG- TAAAATG-3Ј (Ser790 to Ala, plus addition of PstI site).
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ABCC7 p.Ser790Ala 11331356:73:270
status: NEW
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202 Substitution of the two conserved serine residues known to be phosphorylated (Ser686 and Ser790; Picciotto et al., 1992) with alanine residues (S686A/ S790A-XCFTR; Fig. 7, A and C) did not affect the activation by PMA.
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ABCC7 p.Ser790Ala 11331356:202:151
status: NEW
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214 (A) Representative I-V relationships from an oocyte expressing the double knockout of conserved PKC consensus phosphorylation sites (S686A/S790A-XCFTR).
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ABCC7 p.Ser790Ala 11331356:214:139
status: NEW
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224 The data in Fig. 9 indicate that this is not the case because the cAMP-activated currents are not different among oocytes expressing wild-type XCFTR, S686A/ S790A-XCFTR, or T665A/S694A-XCFTR.
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ABCC7 p.Ser790Ala 11331356:224:157
status: NEW
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246 Time course of the currents after stimulation with the cAMP cocktail in oocytes injected with wild-type XCFTR, S686A/S790A-XCFTR, or T665A/S694A-XCFTR cRNAs.
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ABCC7 p.Ser790Ala 11331356:246:117
status: NEW
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PMID: 12588899 [PubMed] Chappe V et al: "Phosphorylation of protein kinase C sites in NBD1 and the R domain control CFTR channel activation by PKA."
No. Sentence Comment
14 To examine if these effects are mediated by direct PKC phosphorylation of CFTR, a mutant was constructed in which serines or threonines at nine PKC consensus sequences on CFTR were replaced by alanines (i.e. the '9CA` mutant T582A/T604A/S641A/T682A/S686A/S707A/S790A/T791A/S809A).
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ABCC7 p.Ser790Ala 12588899:14:261
status: NEW
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145 To distinguish these possible mechanisms we constructed a mutant (9CA) in which all PKC consensus sequences between the Walker B motif of NBD1 and second transmembrane domain (TMD2; i.e. the seventh membrane-spanning segment; T582A, T604A, S641A, T682A, S686A, S707A, S790A, T791A and S809A) were eliminated (Fig. 4A and B).
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ABCC7 p.Ser790Ala 12588899:145:268
status: NEW
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PMID: 18799655 [PubMed] Seavilleklein G et al: "PKC phosphorylation modulates PKA-dependent binding of the R domain to other domains of CFTR."
No. Sentence Comment
256 S686 is a likely candidate to mediate stimulated PKC-dependent interactions since mutation of Ser686 to alanine in the full-length CFTR channel dramatically reduced CFTR activation to the level of 9CA-CFTR (5), whereas mutation of more distal PKC sites in the RD had no effect on the function (S707A/S790A/T791A/S809A).
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ABCC7 p.Ser790Ala 18799655:256:300
status: NEW
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PMID: 10096895 [PubMed] Yamazaki J et al: "Regulation of recombinant cardiac cystic fibrosis transmembrane conductance regulator chloride channels by protein kinase C."
No. Sentence Comment
34 Site-directed mutagenesis The serine at position 686 and/or 790 was modified by polymerase chain reaction-based site-directed mutagenesis (Jones and Howard, 1991) to alanine to create S686A, S790A, and S686 ϩ 790A cardiac CFTR cDNA.
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ABCC7 p.Ser790Ala 10096895:34:191
status: NEW
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283 We examined cAMP and PDBu regulation of cardiac (exon 5-) CFTR channels in oocytes injected with mRNA encoding three mutant constructs: S686A, S790A, and the double mutant S686A-S790A.
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ABCC7 p.Ser790Ala 10096895:283:143
status: NEW
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ABCC7 p.Ser790Ala 10096895:283:178
status: NEW
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284 Fig. 10, A and B, shows representative currents at 70 mV for the S686A and S686A-S790A mutants during exposure to the cAMP cocktail, PDBu, and then a subsequent cAMP cocktail in the continued presence of PDBu.
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ABCC7 p.Ser790Ala 10096895:284:81
status: NEW
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289 This is consistent with a previous report that showed no significant differences in PKA activation sensitivity for the S686A mutant in epithelial CFTR channels (Wilkinson et al., 1996).
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ABCC7 p.Ser790Ala 10096895:289:183
status: NEW
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ABCC7 p.Ser790Ala 10096895:289:240
status: NEW
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291 Normalized PDBu-induced current amplitudes were 55.2 Ϯ 8.8% (n ϭ 4) for wild-type channels, 27.6 Ϯ 5.5% (n ϭ 5) for S686A, 29.0 Ϯ 3.6% (n ϭ 4) for S790A, and 25.1 Ϯ 2.4% (n ϭ 4) for the S686A-S790A double mutant.
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ABCC7 p.Ser790Ala 10096895:291:183
status: NEW
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ABCC7 p.Ser790Ala 10096895:291:240
status: NEW
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315 However, in oo- FIGURE 10 Effects of cAMP and PDBu on cardiac S686A and S790A mutant CFTR channels.
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ABCC7 p.Ser790Ala 10096895:315:72
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316 (A and B) The effects of cAMP cocktail (1ϫ) and PDBu (100 nM) on cardiac CFTR-S686A and CFTR-S686A, S790A were examined using the same protocol as in Fig. 5 A.
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ABCC7 p.Ser790Ala 10096895:316:106
status: NEW
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339 PDBu-induced CFTR current amplitudes were reduced by approximately half in the S686A, S790A, and the double mutant S686A-S790A constructs examined.
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ABCC7 p.Ser790Ala 10096895:339:86
status: NEW
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ABCC7 p.Ser790Ala 10096895:339:121
status: NEW
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281 We examined cAMP and PDBu regulation of cardiac (exon 5afa;) CFTR channels in oocytes injected with mRNA encoding three mutant constructs: S686A, S790A, and the double mutant S686A-S790A.
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ABCC7 p.Ser790Ala 10096895:281:149
status: NEW
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ABCC7 p.Ser790Ala 10096895:281:184
status: NEW
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282 Fig. 10, A and B, shows representative currents at 70 mV for the S686A and S686A-S790A mutants during exposure to the cAMP cocktail, PDBu, and then a subsequent cAMP cocktail in the continued presence of PDBu.
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ABCC7 p.Ser790Ala 10096895:282:81
status: NEW
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313 However, in oo- FIGURE 10 Effects of cAMP and PDBu on cardiac S686A and S790A mutant CFTR channels.
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ABCC7 p.Ser790Ala 10096895:313:72
status: NEW
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314 (A and B) The effects of cAMP cocktail (1afb;) and PDBu (100 nM) on cardiac CFTR-S686A and CFTR-S686A, S790A were examined using the same protocol as in Fig. 5 A.
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ABCC7 p.Ser790Ala 10096895:314:106
status: NEW
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337 PDBu-induced CFTR current amplitudes were reduced by approximately half in the S686A, S790A, and the double mutant S686A-S790A constructs examined.
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ABCC7 p.Ser790Ala 10096895:337:86
status: NEW
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ABCC7 p.Ser790Ala 10096895:337:121
status: NEW
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PMID: 23760269 [PubMed] Billet A et al: "Role of tyrosine phosphorylation in the muscarinic activation of the cystic fibrosis transmembrane conductance regulator (CFTR)."
No. Sentence Comment
102 Carbachol Stimulates CFTR through PKA and Non-PKA Signaling Pathways-To explore PKA-independent regulation of CFTR without using inhibitors that might have confounding effects on other pathways, we studied the activation of 15SA-CFTR (S422A/S660A/S670A/S686A/T690A/S700A/S712A/ S737A/S753A/S768A/T787A/T788A/S790A/S795A/S813A).
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ABCC7 p.Ser790Ala 23760269:102:308
status: NEW
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130 To study PKC regulation without using inhibitors that could perturb other signaling pathways, we used BHK cells expressing 9CA-CFTR, a mutant that lacks all 9 PKC consensus sites in the RD and NBD1 regulatory extension (T582A/T604A/S641A/T682/S686A/S707A/ S790A/T791A/S809A) (13).
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ABCC7 p.Ser790Ala 23760269:130:256
status: NEW
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