ABCMdb

ABCC7 p.Leu1430Ala

None has been submitted yet.

Publications

PMID: 11237860 [PubMed] Hu W et al: "Multiple endocytic signals in the C-terminal tail of the cystic fibrosis transmembrane conductance regulator."

No. Sentence Comment

75 Alanine substitutions in the following mutants were generated by site-directed mutagenesis: K2, F1413A,L1414A; K3, Y1424A,L1430A,L1431A; K6, F1413A; K7, L1414A; K8, Y1424A; K9, L1430A; K10, F16A,F17A (see also Figure 5), by using either single-stranded (for K2, K3, K8 and K9; Muta Gene in itro mutagenesis from Bio-Rad) or double-stranded (for K10; QuickChange site-directed mutagenesis from Stratagene [35]) pcDNA3-TacT-Ct as template. Login to comment
172 The membrane-distal signals, consisting of a canonical Tyr-based motif and a di-Leu motif, were mutated together and designated as mutant K3 (Y1424A,L1430A,L1431A) (Figure 5). Login to comment
200 To evaluate the involvement of single amino acid residues in the membrane-proximal and membrane-distal internalization signals, four additional constructs were prepared that disrupted the three putative endocytic signals individually, as follows: K6, F1413A; K7, L1414A; K8, Y1424A; K9, L1430A (see also Figure 5). Login to comment
231 Mutation of the membrane-distal internalization signals (K8, Y1424A; K9, L1430A) did not interfere with the processing of CFTRM2, as demonstrated by the large-amplitude cAMP-dependent iodide release from cells expressing K3CFTRM2, K8CFTRM2 or K9CFTRM2 (Figure 8A). Login to comment
269 Alanine substitutions of individual residues in the membrane-proximal (K6, F1413A; K7, L1414A) or the membrane-distal (K8, Y1424A; K9, L1430A) stretch revealed an additive effect on the internalization activity (Figure 7D). Login to comment
279 In contrast, the disruption of individual components of the bipartite membrane-distal signal caused a 4-fold (K8, Y1424A) and a 3-fold (K9, L1430A) increase in the cell-surface density of the CFTRM2 (Figure 8B; see also Figure 7D). Login to comment

PMID: 19095655 [PubMed] Kongsuphol P et al: "Mechanistic insight into control of CFTR by AMPK."

No. Sentence Comment

43 EXPERIMENTAL PROCEDURES cRNAs for CFTR and Double Electrode Voltage Clamp-Oocytes were injected with cRNA (10 ng, 47 nl of double-distilled water) encoding wtCFTR, L1430A/L1431A, S573A, S1248A, F508del-CFTR, G551D-CFTR, S768A, S737A, S768D, S737D, E1474X, and AMPK␣1. Login to comment
83 To exclude a nonspecific effect of compound C, we expressed a CFTR mutant (L1430A/ L1431A), which has been proposed to eliminate binding of AMPK␣1 to a C-terminal region of CFTR (5). Login to comment
86 This enhanced activity of L1430A/L1431A-CFTR was similar to that seen with wild-type CFTR first exposed to compound C and then activated by PKA. Login to comment
103 D, summary of whole cell conductances generated by wtCFTR and L1430A/L1431A-CFTR and effects of activators and inhibitors of AMPK. Login to comment
104 E, whole cell currents activated by IBMX and forskolin in wtCFTR and L1430A/L1431A-CFTR expressing oocytes. Login to comment

PMID: 9920908 [PubMed] Prince LS et al: "Efficient endocytosis of the cystic fibrosis transmembrane conductance regulator requires a tyrosine-based signal."

No. Sentence Comment

103 Next, we analyzed CFTR-TR chimeras that contained point mutations in potential internalization signals in both cytoplasmic tail regions: Y38A, L69A, Y1424A, and L1430A (Fig. 1). Login to comment