ABCG2 p.Tyr570Ser
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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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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.Tyr570Ser 25445676:5:120
status: NEW112 We found that mutation of Tyr to Ser at position 469 or 645 resulted in the loss of ATP hydrolysis (even if the activity is corrected for the lower expression level of the Y469S mutant); while mutations in the other two positions apparently did not alter ABCG2 functionality, as both the Y413S and Y570S mutants showed a high level of ATPase activity, which could be inhibited by a general ATPase inhibitor vanadate or the specific ABCG2 inhibitor Ko143 (Fig. 2B).
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ABCG2 p.Tyr570Ser 25445676:112:298
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.Tyr570Ser 25445676:120:54
status: NEW250 BODIPY-prazosin Pheophorbide A Hoechst 33342 mitoxantrone wtABCG2 + + + + Y413S + + + + Y469F + + + + Y570S + + + + Y645F + + + + Fig. 8.
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ABCG2 p.Tyr570Ser 25445676:250:102
status: NEW