ABCB1 p.Tyr1087Phe
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PMID: 24275649
[PubMed]
Loo TW et al: "Locking intracellular helices 2 and 3 together inactivates human P-glycoprotein."
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11
Mutants Y1087A and Y1087L, but not Y1087F, were misprocessed, and all inhibited ATPase activity.
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ABCB1 p.Tyr1087Phe 24275649:11:35
status: NEW148 To test whether Tyr1087 was important for folding or mediating drug stimulation of ATPase activity, we tested the effect of Y1087A, Y1087L, and Y1087F mutations.
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ABCB1 p.Tyr1087Phe 24275649:148:144
status: NEW149 The A52-tagged mutants were expressed in HEK 293 cells in the absence or presence of cyclosporine A, and samples of whole cell SDS extracts were subjected to immunoblot analysis. Fig. 5A shows that the mature 170-kDa protein was the major product in mutant Y1087F, whereas the 150-kDa immature protein was the major product in mutants Y1087A and Y1087L.
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ABCB1 p.Tyr1087Phe 24275649:149:257
status: NEW154 Mutant Y1087F showed about one-third of wild-type P-gp ATPase activity.
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ABCB1 p.Tyr1087Phe 24275649:154:7
status: NEW164 A, A52-tagged Y1087A (A), Y1087F (F), and Y1087L (L) mutants were expressed in the absence (afa;) or presence (af9;) of 5 òe;M cyclosporine A (Cyclo).
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ABCB1 p.Tyr1087Phe 24275649:164:26
status: NEW166 The positions of mature (170-kDa) and immature (150-kDa) P-gps are indicated. B, histidine-tagged WT, Y1087A (A), Y1087F (F), and Y1087L (L) P-gp were expressed in HEK 293 cells and isolated by nickel-chelate chromatography.
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ABCB1 p.Tyr1087Phe 24275649:166:114
status: NEW203 Mutation of Tyr1087 to Leu severely inhibited activity, whereas the conservative Y1087F change caused about a 70% reduction in activity.
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ABCB1 p.Tyr1087Phe 24275649:203:81
status: NEW