ABCG1 p.Lys124Met
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PMID: 22095132
[PubMed]
Tarling EJ et al: "ATP binding cassette transporter G1 (ABCG1) is an intracellular sterol transporter."
No.
Sentence
Comment
101
In contrast, luciferase activity did not increase significantly following overexpression of ABCG1-K124M that contains a mutation in a critical lysine in the Walker A motif (Fig. 5).
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ABCG1 p.Lys124Met 22095132:101:98
status: NEW112 Interestingly, overexpression of the remaining eight ABCG1 constructs failed to induce luciferase activity above the level seen with the ABCG1-K124M mutant (Fig. 5).
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ABCG1 p.Lys124Met 22095132:112:143
status: NEW128 Importantly, this cholesterol-dependent repression of luciferase activity was attenuated in cells overexpressing wild-type ABCG1, but not the inactive mutant ABCG1-K124M (Fig. 6A).
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ABCG1 p.Lys124Met 22095132:128:164
status: NEW148 Further, heterodimeric ABCG5:ABCG8 promotes the efflux of cholesterol ABCG1 -Actin Empty Wildtype K124M G422A F455A Y479A Q498A W511A T513A L534A L541A G569A S573A 8 - 6 - 4 - 2 - 0 - Luciferase(FoldChange) *** *** *** Fig. 5.
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ABCG1 p.Lys124Met 22095132:148:98
status: NEW175 A B C D Luciferase(FoldChange) 1.0 - 0.0 - 0.4 - 0.20.6 - 0.8 - 1.2 - CD CD:25-OHC CD:27-OHCCD:7- OHC CD:7-KetoC NO ABCG1 ABCG1 K124M *** *** Luciferase(FoldChange) 1.0 - 0.0 - 0.4 - 0.2 - 0.6 - 0.8 - 1.2 - 0 0.075 0.25 0.5 1 NO ABCG1 ABCG1 K124M Concentration of 25-OHC ( M) ** * Luciferase(FoldChange) 1.0 - 0.0 - 0.4 - 0.20.6 - 0.8 - NO ABCG1 ABCG1 K124M CD CD:CHOL 1.2 - 1.4 - *** *** * Luciferase(FoldChange) 1.0 - 0.0 - 0.4 - 0.2 - 0.6 - 0.8 - 1.2 - 0 0.075 0.25 0.5 1 NO ABCG1 ABCG1 K124M Concentration of 27-OHC ( M) *** *** *** * Fig. 6.
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ABCG1 p.Lys124Met 22095132:175:128
status: NEWX
ABCG1 p.Lys124Met 22095132:175:241
status: NEWX
ABCG1 p.Lys124Met 22095132:175:352
status: NEWX
ABCG1 p.Lys124Met 22095132:175:490
status: NEW177 (A) CHO-K1 cells were cotransfected with pSynSRE and either wild-type or mutant ABCG1 (ABCG1-K124M).
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ABCG1 p.Lys124Met 22095132:177:93
status: NEW
PMID: 16870176
[PubMed]
Engel T et al: "Expression and functional characterization of ABCG1 splice variant ABCG1(666)."
No.
Sentence
Comment
138
Both, lipoprotein particles as well as serum albumin take up cholesterol twice as efficiently from wt ABCG1 expressing cells as compared to the same cell line where ABCG1 expression had been turned off by application of doxycycline, the parental TetOff HeLa cells or a cell line expressing inactive mutant ABCG1(666; K124M).
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ABCG1 p.Lys124Met 16870176:138:317
status: NEW170 ABCG1(666; K124M) mutant localizes at the cell surface and expression can be regulated by doxycycline.
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ABCG1 p.Lys124Met 16870176:170:11
status: NEW171 TetOff HeLa cells were stable transfected with plasmids coding for wt (HA)3-ABCG1(666), mutant (HA)3-ABCG1(666; K124M) or (HA)3-ABCG2, respectively.
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ABCG1 p.Lys124Met 16870176:171:112
status: NEW174 (B) Lanes 5 and 6: (HA)3-ABCG1(666; K124M) clone 47.
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ABCG1 p.Lys124Met 16870176:174:36
status: NEW184 [3 H]cholesterol efflux to various acceptors was measured for 1.5 h in TetOff HeLa cells either stably transfected with (HA)3-ABCG1(666) (G1-94; white, black), (HA)3-ABCG1(666; K124M) (G1(KM)-47; light/dark grey), or non-transfected (TetOff-HeLa; cross-hatched) in the presence (white, light gray, hatched) or absence (black, dark gray, hatched gray) of 1 lg/ml doxycycline, as described in Section 2. differed from previously characterized ABCG1 variants by absence of an internal segment of 12 amino acids (Fig. 8).
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ABCG1 p.Lys124Met 16870176:184:177
status: NEW204 (A) Samples from TetOff HeLa cell lines expressing wt or mutant (K124M) (HA)3- ABCG transporter, as indicated, were subjected to reducing (right panel) or non-reducing (left panel) SDS-PAGE and subsequent Western blot analysis with HA.11 antibody followed by goat anti-mouse HRP-labeled secondary antibody.
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ABCG1 p.Lys124Met 16870176:204:65
status: NEW206 G1-94, (HA)3-ABCG1(666) clone 94; G1KM-47, (HA)3-ABCG1(666, K124M) clone 47; G2-63, (HA)3-ABCG2 clone 63.
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ABCG1 p.Lys124Met 16870176:206:60
status: NEW235 We thank Dr. Helen Hobbs (UTSW, Dallas, TX, USA) for providing us with an ABCG5-(FLAG)3 plasmid used as a template for cloning ABCG5 employed in control 1_HSG1A 1 SDHKRDLGGDAEVNPFLWHRPSEE------------DSSSMEGCHSFSASCLTQFCILFKRTFL 2_HSG1B 1 SDHKRDLGGDAEVNPFLWHRPSEEVKQTKRLKGLRKDSSSMEGCHSFSASCLTQFCILFKRTFL 3_MMG1_ 1 ADYKRDLGGDTDVNPFLWHRPAEE------------DSASMEGCHSFSASCLTQFCILFKRTFL 4_RNG1_ 1 SDYKRELGGDGDVNPFLWHRPAEE------------DSASMEGCHSFSASCLTQFCILFKRTFL 6_CFG1_ 1 SEHRREPGGDAEVNPFLWHRPSEE------------DSTSMEGCHSFSASCLTQFCILFKRTFL 5_BTG1_ 1 SDCRREPGGDAEVNPFIWHRPSEE------------DSTSMEGCHSFSASCLTQFCILFKRTFL 7_DRG1_ 1 KDYKTEMNGNGVHNPFLWHRPSDE------------DSSSSEGCHSFSASCLTQFCILFKRTFL 8_HSG4_ 1 MAEKKSSPEKNEVPAPCPPCPPEV------------DPIES---HTFATSTLTQFCILFKRTFL hotloop hotloop ordered dis- HSG1A HSG1B A B COOH NH2 Walker B Signature, motif C Walker A outside cytoplasma K124M potential NGS * # 379-VKQTKRLKGLRK-390 Fig. 8.
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ABCG1 p.Lys124Met 16870176:235:863
status: NEW243 The mutated site in the Walker-A motif of the transporter, used for generating ABCG1(666; K124M) mutant, is indicated as well (#).
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ABCG1 p.Lys124Met 16870176:243:90
status: NEW
PMID: 17408620
[PubMed]
Engel T et al: "Expression of ATP binding cassette-transporter ABCG1 prevents cell death by transporting cytotoxic 7beta-hydroxycholesterol."
No.
Sentence
Comment
94
Results In order to identify whether ABCG1 is able to transport oxysterols we used our previously characterized TetOff HeLa cell lines which allow regulatable expression of ABCG1(666) or the ABCG1(666,K124M) defective mutant [16] over four orders of magnitude.
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ABCG1 p.Lys124Met 17408620:94:201
status: NEW
PMID: 24833118
[PubMed]
Engel T et al: "3beta,5alpha,6beta-Cholestanetriol and 25-hydroxycholesterol accumulate in ATP-binding cassette transporter G1 (ABCG1)-deficiency."
No.
Sentence
Comment
37
Cells TetOff-HeLa cell lines TG1-94 and TG1KM-47, stably transfected with pTRE expression plasmids (Clontech) containing wild-type (wt) or K124M-mutant (HA)3-ABCG1(666), respectively [13], were maintained in complete medium (Dulbecco`s modification of Eagle`s medium (DMEM) with 10% fetal calf serum (FCS), antibiotic-antimycotic solution, and glutamine), as previously described [13,14].
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ABCG1 p.Lys124Met 24833118:37:139
status: NEW106 Analysis of ATPase activation by various oxysterols To address the question whether oxysterol species accumulating in Abcg1 deficiency are direct substrates for this transporter, individual oxysterols were applied to tetracycline-inducible HeLa cell lines expressing wt ABCG1 or mutant ABCG1-K124M variant, which was previously shown to be metabolically inactive [13,25].
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ABCG1 p.Lys124Met 24833118:106:292
status: NEW112 As shown in Fig. 2, 25-HC (Fig. 2B, upper right panel), CT (Fig. 2B, lower left panel), and 7b-HC (Fig. 2B, lower right panel) induced MMP in wt ABCG1-expressing cells only (Fig. 2B bold lines), whereas no such effect could be noted in the cells expressing mutant ABCG1-K124M variant (Fig. 2B dashed lines).
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ABCG1 p.Lys124Met 24833118:112:270
status: NEW123 As shown in Fig. 4A, export of 25-HC was enhanced significantly in wt ABCG1-expressing cells, whereas cells expressing mutant ABCG1-K124M were ineffective in this respect.
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ABCG1 p.Lys124Met 24833118:123:132
status: NEW163 Expression of exogenous wt and mutant (K124M) HA3-ABCG1, as well as endogenous ABCG1 in a membrane fraction of cells grown as in (Fig. 4A and B) is shown in (A).
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ABCG1 p.Lys124Met 24833118:163:39
status: NEW167 (B) TetOff HeLa cell lines expressing (bold/dashed line) or not expressing (regular/dotted line) wt ABCG1 (bold/regular line) or mutant ABCG1-K124M (dashed/dotted line), were incubated in the presence of vehicle only (top left panel) or either 5 mM 25-HC (top right panel), 14.2 mM CT (bottom left panel), or 10 mM 7b-HC (bottom right panel), for 24 h. TMRE fluorescence was recorded (see Material and Methods).
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ABCG1 p.Lys124Met 24833118:167:142
status: NEW