ABCG2 p.Tyr469Phe
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PMID: 25445676
[PubMed]
Gal Z et al: "Mutations of the central tyrosines of putative cholesterol recognition amino acid consensus (CRAC) sequences modify folding, activity, and sterol-sensing of the human ABCG2 multidrug transporter."
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5
We found that mutation in Y459 prevented protein expression; the Y469S and Y645S mutants lost their activity; while the Y570S, Y469F, and Y645F mutants retained function as well as cholesterol and bile acid sensitivity.
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ABCG2 p.Tyr469Phe 25445676:5:127
status: NEW114 We found that the Y469F and Y645F mutants were active (Fig. 2B), indicating the importance of the phenyl ring, but not of a hydroxyl group at these positions for protein function.
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ABCG2 p.Tyr469Phe 25445676:114:18
status: NEW120 We found that the basal ATPase activity of the Y469F, Y570S and Y645F mutants showed a moderate (approximately 20%, p b 0.05) increase upon cholesterol addition, while the substrate stimulated ATP hydrolysis of the same mutants was significantly (50-100% increase, p b 0.01) accelerated by cholesterol loading (Fig. 2C).
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ABCG2 p.Tyr469Phe 25445676:120:47
status: NEW174 generated mammalian HEK 293 cells stably expressing the Y413S, Y469F, Y570S and Y645F mutants.
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ABCG2 p.Tyr469Phe 25445676:174:63
status: NEW250 BODIPY-prazosin Pheophorbide A Hoechst 33342 mitoxantrone wtABCG2 + + + + Y413S + + + + Y469F + + + + Y570S + + + + Y645F + + + + Fig. 8.
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ABCG2 p.Tyr469Phe 25445676:250:88
status: NEW