ABCG5 p.Lys92Met
| Predicted by SNAP2: | A: D (91%), C: D (91%), D: D (95%), E: D (95%), F: D (95%), G: D (95%), H: D (95%), I: D (95%), L: D (95%), M: D (91%), N: D (95%), P: D (91%), Q: D (95%), R: D (91%), S: D (95%), T: D (95%), V: D (95%), W: D (95%), Y: D (95%), |
| Predicted by PROVEAN: | A: D, C: D, D: D, E: D, F: D, G: D, H: D, I: D, L: D, M: D, N: D, P: D, Q: D, R: N, S: D, T: D, V: D, W: D, Y: D, |
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[hide] Co-expression of human ABCG5 and ABCG8 in insect c... FEBS Lett. 2006 Nov 13;580(26):6139-44. Epub 2006 Oct 16. Muller M, Klein I, Kopacsi S, Remaley AT, Rajnavolgyi E, Sarkadi B, Varadi A
Co-expression of human ABCG5 and ABCG8 in insect cells generates an androstan stimulated membrane ATPase activity.
FEBS Lett. 2006 Nov 13;580(26):6139-44. Epub 2006 Oct 16., [PMID:17055487]
Abstract [show]
Mutations in the ATP-binding cassette (ABC) proteins ABCG5 or ABCG8 cause sitosterolemia, a condition with increased accumulation of plant sterols. Upon high level expression of the ABCG5 and ABCG8 proteins in baculovirus-Sf9 cell expression system we found a distinct, vanadate sensitive ATPase activity in isolated membrane preparations only when the two proteins were co-expressed. This ATPase activity was significantly stimulated by the addition of certain androgen hormones and analogs, and was effectively inhibited by progesterone. Our results provide a new aspect of biochemical and functional characterization of the ABCG5/ABCG8 proteins and their possible involvement in steroid hormone transport or regulation.
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No. Sentence Comment
57 Co-expression of the wtABCG5 and wtABCG8 as well as K92M-ABCG5 and wtABCG8 was carried out by using different ratios of the corresponding recombinant baculovirus supernatants.
X
ABCG5 p.Lys92Met 17055487:57:52
status: NEW95 As a negative control, we used the co-expression of a Walker A mutant (ABCG5-K92M) of ABCG5 with the wild-type ABCG8 (G5K92M/G8).
X
ABCG5 p.Lys92Met 17055487:95:77
status: NEW118 The specific, androgen-stimulated ATPase activity of the ABCG5/ABCG8 heterodimer was abolished when a key lysine was changed to methionine (K92M) in the Walker A motif of ABCG5.
X
ABCG5 p.Lys92Met 17055487:118:140
status: NEW58 Co-expression of the wtABCG5 and wtABCG8 as well as K92M-ABCG5 and wtABCG8 was carried out by using different ratios of the corresponding recombinant baculovirus supernatants.
X
ABCG5 p.Lys92Met 17055487:58:52
status: NEW96 As a negative control, we used the co-expression of a Walker A mutant (ABCG5-K92M) of ABCG5 with the wild-type ABCG8 (G5K92M/G8).
X
ABCG5 p.Lys92Met 17055487:96:77
status: NEW119 The specific, androgen-stimulated ATPase activity of the ABCG5/ABCG8 heterodimer was abolished when a key lysine was changed to methionine (K92M) in the Walker A motif of ABCG5.
X
ABCG5 p.Lys92Met 17055487:119:140
status: NEW