Liver X receptor alpha

From Wikipedia, the free encyclopedia


Nuclear receptor subfamily 1, group H, member 3
PDB rendering based on 1uhl.
Available structures: 1uhl, 2acl
Identifiers
Symbol(s) NR1H3; LXR-a; LXRA; RLD-1
External IDs OMIM: 602423 MGI: 1352462 HomoloGene: 21165
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 10062 22259
Ensembl ENSG00000025434 ENSMUSG00000002108
Uniprot Q13133 Q91X41
Refseq NM_005693 (mRNA)
NP_005684 (protein)		 NM_013839 (mRNA)
NP_038867 (protein)
Location Chr 11: 47.23 - 47.25 Mb Chr 2: 90.98 - 91 Mb
Pubmed search [1] [2]

Liver X receptor alpha (LXR-alpha) is a nuclear receptor protein encoded by the NR1H3 gene (nuclear receptor subfamily 1, group H, member 3).[1][2]

[edit] References

  1. ^ Miyata KS, McCaw SE, Patel HV, Rachubinski RA, Capone JP (1996). "The orphan nuclear hormone receptor LXR alpha interacts with the peroxisome proliferator-activated receptor and inhibits peroxisome proliferator signaling". J. Biol. Chem. 271 (16): 9189–92. doi:10.1074/jbc.271.16.9189. PMID 8621574. 
  2. ^ Willy PJ, Umesono K, Ong ES, Evans RM, Heyman RA, Mangelsdorf DJ (1995). "LXR, a nuclear receptor that defines a distinct retinoid response pathway". Genes Dev. 9 (9): 1033–45. doi:10.1101/gad.9.9.1033. PMID 7744246. 

[edit] Further reading

  • Willy PJ, Umesono K, Ong ES, et al. (1995). "LXR, a nuclear receptor that defines a distinct retinoid response pathway.". Genes Dev. 9 (9): 1033–45. PMID 7744246. 
  • Miyata KS, McCaw SE, Patel HV, et al. (1996). "The orphan nuclear hormone receptor LXR alpha interacts with the peroxisome proliferator-activated receptor and inhibits peroxisome proliferator signaling.". J. Biol. Chem. 271 (16): 9189–92. PMID 8621574. 
  • Lehmann JM, Kliewer SA, Moore LB, et al. (1997). "Activation of the nuclear receptor LXR by oxysterols defines a new hormone response pathway.". J. Biol. Chem. 272 (6): 3137–40. PMID 9013544. 
  • Auboeuf D, Rieusset J, Fajas L, et al. (1997). "Tissue distribution and quantification of the expression of mRNAs of peroxisome proliferator-activated receptors and liver X receptor-alpha in humans: no alteration in adipose tissue of obese and NIDDM patients.". Diabetes 46 (8): 1319–27. PMID 9231657. 
  • Peet DJ, Turley SD, Ma W, et al. (1998). "Cholesterol and bile acid metabolism are impaired in mice lacking the nuclear oxysterol receptor LXR alpha.". Cell 93 (5): 693–704. PMID 9630215. 
  • Miyata KS, McCaw SE, Meertens LM, et al. (1999). "Receptor-interacting protein 140 interacts with and inhibits transactivation by, peroxisome proliferator-activated receptor alpha and liver-X-receptor alpha.". Mol. Cell. Endocrinol. 146 (1-2): 69–76. PMID 10022764. 
  • Venkateswaran A, Laffitte BA, Joseph SB, et al. (2000). "Control of cellular cholesterol efflux by the nuclear oxysterol receptor LXR alpha.". Proc. Natl. Acad. Sci. U.S.A. 97 (22): 12097–102. doi:10.1073/pnas.200367697. PMID 11035776. 
  • Chinetti G, Lestavel S, Bocher V, et al. (2001). "PPAR-alpha and PPAR-gamma activators induce cholesterol removal from human macrophage foam cells through stimulation of the ABCA1 pathway.". Nat. Med. 7 (1): 53–8. doi:10.1038/83348. PMID 11135616. 
  • Laffitte BA, Repa JJ, Joseph SB, et al. (2001). "LXRs control lipid-inducible expression of the apolipoprotein E gene in macrophages and adipocytes.". Proc. Natl. Acad. Sci. U.S.A. 98 (2): 507–12. doi:10.1073/pnas.021488798. PMID 11149950. 
  • Li Y, Bolten C, Bhat BG, et al. (2002). "Induction of human liver X receptor alpha gene expression via an autoregulatory loop mechanism.". Mol. Endocrinol. 16 (3): 506–14. PMID 11875109. 
  • Mak PA, Laffitte BA, Desrumaux C, et al. (2002). "Regulated expression of the apolipoprotein E/C-I/C-IV/C-II gene cluster in murine and human macrophages. A critical role for nuclear liver X receptors alpha and beta.". J. Biol. Chem. 277 (35): 31900–8. doi:10.1074/jbc.M202993200. PMID 12032151. 
  • Brendel C, Gelman L, Auwerx J (2003). "Multiprotein bridging factor-1 (MBF-1) is a cofactor for nuclear receptors that regulate lipid metabolism.". Mol. Endocrinol. 16 (6): 1367–77. PMID 12040021. 
  • Steffensen KR, Schuster GU, Parini P, et al. (2002). "Different regulation of the LXRalpha promoter activity by isoforms of CCAAT/enhancer-binding proteins.". Biochem. Biophys. Res. Commun. 293 (5): 1333–40. doi:10.1016/S0006-291X(02)00390-X. PMID 12054659. 
  • Gbaguidi GF, Agellon LB (2002). "The atypical interaction of peroxisome proliferator-activated receptor alpha with liver X receptor alpha antagonizes the stimulatory effect of their respective ligands on the murine cholesterol 7alpha-hydroxylase gene promoter.". Biochim. Biophys. Acta 1583 (2): 229–36. PMID 12117567. 
  • Pawar A, Xu J, Jerks E, et al. (2002). "Fatty acid regulation of liver X receptors (LXR) and peroxisome proliferator-activated receptor alpha (PPARalpha ) in HEK293 cells.". J. Biol. Chem. 277 (42): 39243–50. doi:10.1074/jbc.M206170200. PMID 12161442. 
  • Brendel C, Schoonjans K, Botrugno OA, et al. (2003). "The small heterodimer partner interacts with the liver X receptor alpha and represses its transcriptional activity.". Mol. Endocrinol. 16 (9): 2065–76. PMID 12198243. 
  • Oberkofler H, Schraml E, Krempler F, Patsch W (2003). "Potentiation of liver X receptor transcriptional activity by peroxisome-proliferator-activated receptor gamma co-activator 1 alpha.". Biochem. J. 371 (Pt 1): 89–96. doi:10.1042/BJ20021665. PMID 12470296. 
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932. 
  • Wang M, Thomas J, Burris TP, et al. (2004). "Molecular determinants of LXRalpha agonism.". J. Mol. Graph. Model. 22 (2): 173–81. doi:10.1016/S1093-3263(03)00159-1. PMID 12932788. 
  • Fukuchi J, Song C, Ko AL, Liao S (2004). "Transcriptional regulation of farnesyl pyrophosphate synthase by liver X receptors.". Steroids 68 (7-8): 685–91. PMID 12957674. 
 This article on a gene on chromosome 11 is a stub. You can help Wikipedia by expanding it.
v • d • e
Transcription factors and intracellular receptors
(1) Basic domains
(1.1) Basic leucine zipper (bZIP)
Activating transcription factor (AATF, 1, 2, 3, 4, 5, 6, 7) • AP-1 (c-Fos, FOSB, FOSL1, FOSL2, c-Jun, JUNB, JUND) • BACH (1, 2) • BATF • BLZF1 • C/EBP (α, β, γ, δ, ε, ζ) • CREB (1, 3, L1) • CREM • DBP • DDIT3 • GABPA • HLF • MAF (B, F, G, K) • NFE (2, L1, L2) • NRL • NRF1 • XBP1
(1.2) Basic helix-loop-helix (bHLH)
ATOH1 • AhR • AHRR • ARNT • ASCL1 • BHLHB2 • BMAL (ARNTL, ARNTL2) • CLOCK • EPAS1 • HAND (1, 2) • HES (5, 6) • HEY (1, 2, L) • HES1 • HIF (1A, 3A) • ID (1, 2, 3, 4) • LYL1 • MXD4 • MYCL1 • MYCN • Myogenic regulatory factors (MyoD, Myogenin, MYF5, MYF6) • Neurogenins • NeuroD (1, 2) • NPAS (1, 2, 3) • OLIG (1, 2) • Scleraxis • TAL1 • Twist • USF1
(1.3) bHLH-ZIP
MAX • MITF • MNT • MLX • MXI1 • Myc • SREBP (1, 2)
(1.6) Basic helix-span-helix (bHSH)
(2) Zinc finger
DNA-binding domains
(2.1) Nuclear receptor (Cys4)
subfamily 1 (Thyroid hormone (α, β), CAR, FXR, LXR (α, β), PPAR (α, β/δ, γ), PXR, RAR (α, β, γ), ROR (α, β, γ), Rev-ErbA (α, β), VDR) • subfamily 2 (COUP-TF (I, II), Ear-2, HNF4 (α, γ), PNR, RXR (α, β, γ), Testicular receptor (2, 4), TLX) • subfamily 3 (Steroid hormone (Estrogen (α, β), Estrogen related (α, β, γ), Androgen, Glucocorticoid, Mineralocorticoid, Progesterone)) • subfamily 4 NUR (NGFIB, NOR1, NURR1) • subfamily 5 (LRH-1, SF1) • subfamily 6 (GCNF) • subfamily 0 (DAX1, SHP)
(2.2) Other Cys4
GATA (1, 2, 3, 4, 5, 6) • MTA (1, 2, 3)
(2.3) Cys2His2
ATBF1 • BCL(6, 11A, 11B) • CTCF • E4F1 • EGR (2, 3) • ERV3 • General transcription factors (TFIIA, TFIIB, TFIID, TFIIE, TFIIF: 1, 2, TFIIH: 1, 2, 4, 2I, 3A, 3C1, 3C2) • GFI1 • GLI-Krüppel family (1, 2, 3, YY1) • HIC (1, 2) • HIVEP (1, 2, 3) • IKZF (1, 2, 3) • ILF (2, 3) • KLF (2, 4, 5, 6, 9, 10, 11, 12, 13) • MTF1 • MYT1 • OSR1 • Sp1 • zinc finger ((3, 7, 9, 10, 19, 22, 24, 33B, 34, 35, 41, 43, 44, 51, 74, 143, 146, 148, 165, 202, 217, 219, 238, 239, 259, 267, 268, 281, 295, 318, 330, 346, 350, 365, 366, 384, 451, 452, 471, 593, 638, 649, 655) • Zbtb7 (7A) • ZBT (16, 17, 33)
(2.4) Cys6
(2.5) Alternating composition
AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B
(3) Helix-turn-helix
domains
ARX • CDX (1, 2) • CRX • CUTL1 • DLX (3, 4, 5) • EMX2 • EN (1, 2) • FHL (1, 2, 3) • HESX1 • HHEX • HLX • Homeobox (A1, A3, A4, A5, A7, A9, A10, A11, A13, B1, B2, B3, B4, B5, B6, B7, B8, B9, B13, C4, C5, C6, C8, C9, C10, C11, C13, D1, D3, D4, D8, D9, D10, D11, D12, D13) • HOPX • MEIS (1, 2) • MEOX2 • MNX1 • MSX (1, 2) • NANOG • NKX (2-1, 2-5, 3-1) • PHF (3, 6, 10, 17) • POU domain (PIT-1, BRN-3: 1, 2, Octamer transcription factor: 1, 2, 3/4, 6, 7) • OTX (1, 2) • PDX1
(3.2) Paired box
PAX (1, 2, 3, 4, 5, 6, 7, 8, 9)
E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, , O3A, O4, P1, P2, P3)
HSF (1, 2, 4)
(3.5) Tryptophan clusters
ELF (4, 5) • EGF • ELK (1, 3, 4) • ERF • ERG • ETS (1, 2) • ETV (1, 4, 5, 6) • FLI1 • Interferon regulatory factors (1, 2, 3, 4, 5, 6, 7, 8) • MYB • MYBL2
(3.6) TEA domain
transcriptional enhancer factor 1, 2
(4) β-Scaffold factors with
minor groove contacts
(4.1) Rel homology region
NF-κB (NFKB1, NFKB2, REL, RELA, RELB) • NFAT (C1, C2, C3, C4, 5)
(4.2) STAT
STAT (1, 2, 3, 4, 5, 6)
(4.3) p53
(4.4) MADS box
Mef2 (A, B, C, D) • SRF
HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 13, 15, 18) • SRY • SSRP1
(4.10) Cold-shock domain
(4.11) Runt
(0) Other
transcription factors
(0.2) HMGI(Y)
HMGA (1, 2) • HBP1
Rb • RBL1 • RBL2
(0.5) AP-2/EREBP-related factors
Apetala 2 • EREBP • B3
(0.6) Miscellaneous
ARID (1A, 1B, 2, 3A, 3B, 4A) • CAP • IFI (16, 35) • MLL (2, 3, T1) • MNDA • NFI (A, B, C, X) • NFY (A, B, C) • Rho/Sigma • R-SMAD