ABCA1 p.Leu2251Ala

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PMID: 21507939 [PubMed] Hozoji-Inada M et al: "Liver X receptor beta (LXRbeta) interacts directly with ATP-binding cassette A1 (ABCA1) to promote high density lipoprotein formation during acute cholesterol accumulation."
No. Sentence Comment
90 However, mutation of Leu2247 and Leu2251 to alanine abrogated the co-precipitation of LXRbeta despite comparable levels of expression among these mutants and WT ABCA1.
X
ABCA1 p.Leu2251Ala 21507939:90:33
status: NEW
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108 HEK293 cells stably expressing FLAG-tagged LXRbeta were transfected with HA-tagged WT ABCA1 L2247A mutant or L2251A mutant.
X
ABCA1 p.Leu2251Ala 21507939:108:109
status: NEW
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113 When the mutant constructs were expressed in HEK293 cells, L2247A or L2251A substitution did not affect the surface expression of ABCA1, but LXRbeta no longer co-localized with ABCA1 (Fig. 2).
X
ABCA1 p.Leu2251Ala 21507939:113:69
status: NEW
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120 Interestingly, apoA-I bound to cells expressing L2247A or L2251A mutant ABCA1 even when LXRbeta was co-expressed.
X
ABCA1 p.Leu2251Ala 21507939:120:58
status: NEW
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122 When ABCA1-L2247A, ABCA1-L2251A, or ABCA1-L2247A/L2251A was expressed alone, cholesterol efflux to apoA-I was comparable with cells expressing WT ABCA1 in the absence or presence of TO901317 (black bars and empty bars, respectively, in Fig. 3B).
X
ABCA1 p.Leu2251Ala 21507939:122:25
status: NEW
X
ABCA1 p.Leu2251Ala 21507939:122:49
status: NEW
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126 Co-expression of LXRbeta doubled the plasma membrane levels of WT ABCA1 as shown previously (16), but surface levels of the mutants (L2247A, L2251A, and L2247/L2251A) were not affected by LXRbeta expression (Fig. 3C).
X
ABCA1 p.Leu2251Ala 21507939:126:141
status: NEW
X
ABCA1 p.Leu2251Ala 21507939:126:159
status: NEW
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149 ABCA1-L2247A/L2251A double mutant was labeled as efficiently as WT ABCA1 (lane 9), but this was not inhibited by LXRbeta co-expression (lanes 11 and 12), suggesting that the interaction of LXRbeta with ABCA1 via Leu2247 and Leu2251 prevents tight ATP binding.
X
ABCA1 p.Leu2251Ala 21507939:149:13
status: NEW
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89 However, mutation of Leu2247 and Leu2251 to alanine abrogated the co-precipitation of LXRbeta despite comparable levels of expression among these mutants and WT ABCA1.
X
ABCA1 p.Leu2251Ala 21507939:89:33
status: NEW
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107 HEK293 cells stably expressing FLAG-tagged LXRbeta were transfected with HA-tagged WT ABCA1 L2247A mutant or L2251A mutant.
X
ABCA1 p.Leu2251Ala 21507939:107:109
status: NEW
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112 When the mutant constructs were expressed in HEK293 cells, L2247A or L2251A substitution did not affect the surface expression of ABCA1, but LXRbeta no longer co-localized with ABCA1 (Fig. 2).
X
ABCA1 p.Leu2251Ala 21507939:112:69
status: NEW
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119 Interestingly, apoA-I bound to cells expressing L2247A or L2251A mutant ABCA1 even when LXRbeta was co-expressed.
X
ABCA1 p.Leu2251Ala 21507939:119:58
status: NEW
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121 When ABCA1-L2247A, ABCA1-L2251A, or ABCA1-L2247A/L2251A was expressed alone, cholesterol efflux to apoA-I was comparable with cells expressing WT ABCA1 in the absence or presence of TO901317 (black bars and empty bars, respectively, in Fig. 3B).
X
ABCA1 p.Leu2251Ala 21507939:121:25
status: NEW
X
ABCA1 p.Leu2251Ala 21507939:121:49
status: NEW
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125 Co-expression of LXRbeta doubled the plasma membrane levels of WT ABCA1 as shown previously (16), but surface levels of the mutants (L2247A, L2251A, and L2247/L2251A) were not affected by LXRbeta expression (Fig. 3C).
X
ABCA1 p.Leu2251Ala 21507939:125:141
status: NEW
X
ABCA1 p.Leu2251Ala 21507939:125:159
status: NEW
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148 ABCA1-L2247A/L2251A double mutant was labeled as efficiently as WT ABCA1 (lane 9), but this was not inhibited by LXRbeta co-expression (lanes 11 and 12), suggesting that the interaction of LXRbeta with ABCA1 via Leu2247 and Leu2251 prevents tight ATP binding.
X
ABCA1 p.Leu2251Ala 21507939:148:13
status: NEW
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