ABCB1 p.Phe343Arg
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PMID: 17848563
[PubMed]
Loo TW et al: "Suppressor mutations in the transmembrane segments of P-glycoprotein promote maturation of processing mutants and disrupt a subset of drug-binding sites."
No.
Sentence
Comment
1
The folding defect in ⌬F508 cystic fibrosis transmembrane conductance regulator might be correctable because misfolding of a P-glycoprotein (P-gp; ABCB1) mutant lacking the equivalent residue (⌬Y490) could be corrected with drug substrates or by introduction of an arginine residue into transmembrane (TM) segments 5 (I306R) or 6 (F343R).
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ABCB1 p.Phe343Arg 17848563:1:345
status: NEW7 The presence of arginine residues reduced the apparent affinity of P-gp for vinblastine (L65R, T199R, and I306R), cyclosporin (I306R and F343R), or rhodamine B (F343R) by 4-60-fold.
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ABCB1 p.Phe343Arg 17848563:7:137
status: NEWX
ABCB1 p.Phe343Arg 17848563:7:161
status: NEW40 Printed in the U.S.A. NOVEMBER 2, 2007•VOLUME 282•NUMBER 44 JOURNAL OF BIOLOGICAL CHEMISTRY 32043 essing mutants by a direct mechanism because suppressor mutations (arginines) introduced into TM segments 5 (I306R) and 6 (F343R) also promoted maturation of the protein (21).
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ABCB1 p.Phe343Arg 17848563:40:236
status: NEW69 For disulfide cross-linking analysis, the cDNA of mutant L339C(TM6)/ F728C(TM7) (34) was modified to also encode the L65R, T199R, I306R, or F343R mutations.
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ABCB1 p.Phe343Arg 17848563:69:140
status: NEW102 By contrast, mutant F343R/⌬Y490 yielded about equivalent amounts of the mature 170-kDa and immature 150-kDa proteins and very little 130-kDa product.
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ABCB1 p.Phe343Arg 17848563:102:20
status: NEW103 Therefore, the presence of arginine mutations in TM5 (I306R) or TM6 (F343R) might have promoted maturation of ⌬Y490 P-gp by influencing distal folding events.
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ABCB1 p.Phe343Arg 17848563:103:69
status: NEW165 Processing mutant G251V was chosen because it yields very low levels of mature 170-kDa protein and could be rescued by the presence of arginine in TM5 (I306R) or in TM6 (F343R) (21).
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ABCB1 p.Phe343Arg 17848563:165:170
status: NEW236 The F343R mutation exhibited decreased apparent affinity for rhodamine B (3.6-fold) and cyclosporin A (18-fold) but not for vinblastine (Ͻ2-fold).
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ABCB1 p.Phe343Arg 17848563:236:4
status: NEW
No.
Sentence
Comment
261
Loo et al. (2007) observed that mutation of Phe343 to arginine reduced the affinity of P-gp for rhodamine B and cyclosporine A, but not for vinblastine.
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ABCB1 p.Phe343Arg 25264938:261:44
status: NEW
PMID: 26507655
[PubMed]
Loo TW et al: "Mapping the Binding Site of the Inhibitor Tariquidar That Stabilizes the First Transmembrane Domain of P-glycoprotein."
No.
Sentence
Comment
176
One arginine mutation predicted to line the drug-binding pocket inhibited rescue in TM2 (A129R) (Fig. 4B) and two arginines predicted to line the drug-binding pocket in TM6 (F336R and F343R) were FIGURE 4.
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ABCB1 p.Phe343Arg 26507655:176:184
status: NEW194 The other 12 mutants in TM1 (F72R), TM5 (Y307R and Y310R), TM6 (F336R and F343R), TM7 (F732R), TM10 (V865R), TM11 (M949R, Y950R, S952R, and Y953R), and TM12 (L975R and F978R) were not rescued by cyclosporine A (Fig. 7).
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ABCB1 p.Phe343Arg 26507655:194:74
status: NEW283 We identified 13 additional arginine mutations (H61R, G64R, L65R, and M68R in TM1; A129R in TM2; I306R and S309R in TM5; F343R in TM6; F942R, T945R, Q946R, and Y950R in TM11; and L975R in TM12) (Fig. 11A) that were not predicted to lie within 4.5-&#c5; of the predicted site 3 tariquidar-binding site (9).
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ABCB1 p.Phe343Arg 26507655:283:121
status: NEW