ABCB1 p.Gly269Val
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PMID: 10506575
[PubMed]
Loo TW et al: "The human multidrug resistance P-glycoprotein is inactive when its maturation is inhibited: potential for a role in cancer chemotherapy."
No.
Sentence
Comment
64
Accordingly, the histidine-tagged 150 kDa protein of mutants G268V, G269V, and Y710A were isolated (Fig. 1, lanes 1, 3, and 5).
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ABCB1 p.Gly269Val 10506575:64:68
status: NEW66 To convert the processing mutants G268V, G269V, and Y710A to the mature enzyme, the mutants were synthesized in the presence of 10 M cyclosporin A to induce maturation (19).
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ABCB1 p.Gly269Val 10506575:66:41
status: NEW73 As reported previously (19), the mature enzyme of mutants G268V and G269V had ϳ50 to 75% of the activity of wild-type P-gp.
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ABCB1 p.Gly269Val 10506575:73:68
status: NEW76 ATPase activity of P-gp that is prevented from undergoing maturation It was possible that the 150 kDa core-glycosylated P-gp of the processing mutants G268V, G269V, and Y710A were inactive because the point mutations inherently caused misfolding of the protein and subsequent retention in the endoplasmic reticulum.
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ABCB1 p.Gly269Val 10506575:76:158
status: NEW84 Equivalent amounts of histidine-tagged mature and core-glycosylated P-gp of wild-type and mutants G268V, G269V, and Y710A, isolated by nickel-chelate chromatography, were reconstituted with lipid and assayed for verapamil- (1 mM) and vinblastine- (0.05 mM) stimulated ATPase activities.
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ABCB1 p.Gly269Val 10506575:84:105
status: NEW88 HEK293 cells expressing histidine-tagged P-gp mutants G268V, G269V or Y710A were incubated with (ϩ) or without (-) 10 M cyclosporin A (cyclo) for 24 h. The cells were harvested and solubilized with n-dodecyl-beta-D-maltoside and the cell extracts were subjected to nickel-chelate chromatography with 20 mM imidazole in the wash buffers.
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ABCB1 p.Gly269Val 10506575:88:61
status: NEW
PMID: 9829963
[PubMed]
Loo TW et al: "Quality control by proteases in the endoplasmic reticulum. Removal of a protease-sensitive site enhances expression of human P-glycoprotein."
No.
Sentence
Comment
117
By contrast, the core-glycosylated G268V protein failed to mature and was almost undetectable by 24 h. In the double mutant (G268V ϩ R113A), however, there was a 5-10-fold increase in the amount of P-gp at 0 h, but the mutant still failed to mature and was degraded by 24 h. A similar pattern was observed for the processing mutant G269V (data not shown).
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ABCB1 p.Gly269Val 9829963:117:338
status: NEW
PMID: 23733192
[PubMed]
Loo TW et al: "Human P-glycoprotein contains a greasy ball-and-socket joint at the second transmission interface."
No.
Sentence
Comment
96
The I261S, V264S, F267A, G268V, and G269V mutations blocked maturation such that the 150-kDa immature protein was the major product (Fig. 1B).
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ABCB1 p.Gly269Val 23733192:96:36
status: NEW
PMID: 25987565
[PubMed]
Loo TW et al: "The Transmission Interfaces Contribute Asymmetrically to the Assembly and Activity of Human P-glycoprotein."
No.
Sentence
Comment
152
Asymmetry of the P-gp Drug Pump Transmission Interfaces JULY 3, 2015ߦVOLUME 290ߦNUMBER 27 JOURNAL OF BIOLOGICAL CHEMISTRY 16957 at SEMMELWEIS UNIV OF MEDICINE on December 4, twenty-eight mutations in ICL2 (A250L, G251V, V253S, A254L, E256A, L258S, I261S, V264S, F267A, G268V, G269V, L274S, R276A, Y277A) inhibited maturation of P-gp (b0d;15% mature P-gp) while four other ICL2 mutations (A2650L, R262A, T263A, and I265S) partially reduced maturation of P-gp (about 55-60% mature P-gp).
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ABCB1 p.Gly269Val 25987565:152:289
status: NEW