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Details on Person In addition to its well defined role as a transcription fact...

Class:IdSummation:9619759
_displayNameIn addition to its well defined role as a transcription fact...
_timestamp2019-08-14 03:03:23
created[InstanceEdit:9619758] Shamovsky, Veronica, 2018-09-18
literatureReference[LiteratureReference:9621107] Direct interaction of nuclear liver X receptor-beta with ABCA1 modulates cholesterol efflux
[LiteratureReference:9621108] Liver X receptor beta (LXRbeta) interacts directly with ATP-binding cassette A1 (ABCA1) to promote high density lipoprotein formation during acute cholesterol accumulation
modified[InstanceEdit:9629128] Shamovsky, Veronica, 2018-11-19
[InstanceEdit:9634037] Shamovsky, Veronica, 2019-01-03
[InstanceEdit:9657834] Shamovsky, Veronica, 2019-08-09
[InstanceEdit:9658282] Shamovsky, Veronica, 2019-08-12
[InstanceEdit:9658425] Shamovsky, Veronica, 2019-08-14
textIn addition to its well defined role as a transcription factor, liver X receptor β (LXRβ or NR1H2) can directly bind to the C-terminal region of ATP-binding cassette A1 (ABCA1) in the human macrophage-like (THP-1) and human embryonic kidney 293 (HEK293) cell lines to impact ABCA1 protein function (Hozoji M et al. 2008; Hozoji-Inada M et al. 2011). In the absence of cholesterol accumulation in THP-1 cells, the ABCA1:NR1H2 complex stably localizes to the plasma membrane, but apolipoprotein A-I (apoA-I) binding or cholesterol efflux does not occur (Hozoji M et al. 2008; Hozoji-Inada M et al. 2011). Exogenously added NR1H2 ligands, which mimic cholesterol accumulation, cause NR1H2 (LXRβ) to dissociate from ABCA1, thus freeing ABCA1 for apoA-I binding and subsequent cholesterol efflux (Hozoji M et al. 2008; Hozoji-Inada M et al. 2011). Photoaffinity labeling experiments with 8-azido-[α-(32)P]ATP suggested that the interaction of NR1H2 (LXRβ) with ABCA1 inhibits ATP binding by ABCA1 (Hozoji-Inada M et al. 2011).
(summation)[Reaction:9619756] NR1H2 binds ABCA1 [Homo sapiens]
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