Difference between revisions of "Part:BBa K4164003"

Revision as of 14:18, 7 October 2022

Retinoid X receptor-alpha(RXRα)

Retinoid X receptor alpha (RXR-alpha), also known as NR2B1 (nuclear receptor subfamily 2, group B, member 1) is a nuclear receptor that in humans is encoded by the RXRA gene.

RXRs are associated with multiple cellular processes from cell proliferation to cell metabolism. RXRs have the ability to form heterodimers with subfamily 1 nuclear receptors including CAR, FXR, LXR, PPAR， PXR， RAR， TR and VDR.

As with other type II nuclear receptors, the RXR heterodimer in the absence of ligand is bound to hormone response elements complexed with corepressor proteins. Binding of agonist ligands to RXR results in dissociation of corepressor and recruitment of coactivator protein, which, in turn, promotes transcription of the downstream target gene into mRNA and eventually protein. Alternatively, binding of RXR ligands to heterodimers can stimulate transcriptional activation of RXR chaperone receptors. For example, when binding as a heterodimer with bile acid-activated FXR in liver cells, it will regulate the metabolic processes of bile acid (BA), lipid, and glucose.

In our project, we took advantage of the characteristics that RXR can bind to the farnesoid X receptor(FXR) as a heterodimer, using FXR as the receptor, and when activated by de-sulfated CDCA-S, it will form a heterodimeric complex with the FXR, so that the downstream ddRFP-A1 and ddRFP-B1 are correspondingly driven to dimerize and emit fluorescence.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
INCOMPATIBLE WITH RFC[25]
Illegal NgoMIV site found at 357
1000
INCOMPATIBLE WITH RFC[1000]
Illegal BsaI.rc site found at 739

@@ Line 7: / Line 7: @@
 RXRs are associated with multiple cellular processes from cell proliferation to cell metabolism. RXRs have the ability to form heterodimers with subfamily 1 nuclear receptors including CAR, FXR, LXR, PPAR， PXR， RAR， TR and VDR.
-As with other type II nuclear receptors, the RXR heterodimer in the absence of ligand is bound to hormone response elements complexed with corepressor proteins. Binding of agonist ligands to RXR results in dissociation of corepressor and recruitment of coactivator protein, which, in turn, promotes transcription of the downstream target gene into mRNA and eventually protein.
+As with other type II nuclear receptors, the RXR heterodimer in the absence of ligand is bound to hormone response elements complexed with corepressor proteins. Binding of agonist ligands to RXR results in dissociation of corepressor and recruitment of coactivator protein, which, in turn, promotes transcription of the downstream target gene into mRNA and eventually protein. Alternatively, binding of RXR ligands to heterodimers can stimulate transcriptional activation of RXR chaperone receptors. For example, when binding as a heterodimer with bile acid-activated FXR in liver cells, it will regulate the metabolic processes of bile acid (BA), lipid, and glucose.
-Alternatively, binding of RXR ligands to heterodimers can stimulate transcriptional activation of RXR chaperone receptors.
-For example, when binding as a heterodimer with bile acid-activated FXR in liver cells, it will regulate the metabolic processes of bile acid (BA), lipid, and glucose.
 In our project, we took advantage of the characteristics that RXR can bind to the farnesoid X receptor(FXR) as a heterodimer, using FXR as the receptor, and when activated by de-sulfated CDCA-S, it will form a heterodimeric complex with the FXR, so that the downstream ddRFP-A1 and ddRFP-B1 are correspondingly driven to dimerize and emit fluorescence.