ABCC7 p.Thr791Ala
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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.Thr791Ala 12588899:14:267
status: NEW145 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.Thr791Ala 12588899:145:275
status: NEW
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.Thr791Ala 18799655:256:306
status: NEW
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
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.Thr791Ala 23760269:130:262
status: NEW