Farnesoid X receptor

From Wikipedia, the free encyclopedia

Nuclear receptor subfamily 1, group H, member 4

PDB rendering based on 1osh.

Available structures: 1osh, 1osv, 1ot7

Identifiers

Symbol(s)

NR1H4; BAR; FXR; HRR-1; HRR1; MGC163445; RIP14

External IDs

OMIM: 603826 MGI: 1352464 HomoloGene: 3760

Gene ontology
Molecular Function:	• transcription factor activity • steroid hormone receptor activity • transcription coactivator activity • transcription corepressor activity • protein binding • zinc ion binding • sequence-specific DNA binding • metal ion binding
Cellular Component:	• nucleus
Biological Process:	• transcription • regulation of transcription, DNA-dependent • signal transduction • bile acid metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_005123 (mRNA)
NP_005114 (protein)

NM_009108 (mRNA)
NP_033134 (protein)

Location

Chr 12: 99.39 - 99.48 Mb

n/a

Pubmed search

[1]

[2]

The farnesoid X receptor (FXR), also known as NR1H4 (nuclear receptor subfamily 1, group H, member 4) is a nuclear hormone receptor with activity similar to that seen in other steroid receptors such as estrogen or progesterone but more similar in form to PPAR, LXR and RXR. FXR is encoded by the NR1H4 gene.^[1]

Chenodeoxycholic acid and other bile acids are the natural ligand for FXR and like other steroid receptors, when activated, it translocates to the cell nucleus, forms a dimer (in this case a heterodimer) and binds to hormone response elements on DNA which elicits expression or transrepression of gene products. One of the primary functions of FXR activation is the suppression of cholesterol 7 alpha-hydroxylase (CYP7A1), the rate-limiting enzyme in bile acid synthesis from cholesterol.

[edit] References

^ Entrez Gene: NR1H4 nuclear receptor subfamily 1, group H, member 4.

[edit] Further reading

Kalaany NY, Mangelsdorf DJ (2006). "LXRS and FXR: the yin and yang of cholesterol and fat metabolism.". Annu. Rev. Physiol. 68: 159–91. doi:10.1146/annurev.physiol.68.033104.152158. PMID 16460270.
Kuipers F, Stroeve JH, Caron S, Staels B (2007). "Bile acids, farnesoid X receptor, atherosclerosis and metabolic control.". Curr. Opin. Lipidol. 18 (3): 289–97. doi:10.1097/MOL.0b013e3281338d08. PMID 17495603.
Seol W, Choi HS, Moore DD (1995). "Isolation of proteins that interact specifically with the retinoid X receptor: two novel orphan receptors.". Mol. Endocrinol. 9 (1): 72–85. PMID 7760852.
Forman BM, Goode E, Chen J, et al. (1995). "Identification of a nuclear receptor that is activated by farnesol metabolites.". Cell 81 (5): 687–93. PMID 7774010.
Zavacki AM, Lehmann JM, Seol W, et al. (1997). "Activation of the orphan receptor RIP14 by retinoids.". Proc. Natl. Acad. Sci. U.S.A. 94 (15): 7909–14. PMID 9223286.
Makishima M, Okamoto AY, Repa JJ, et al. (1999). "Identification of a nuclear receptor for bile acids.". Science 284 (5418): 1362–5. PMID 10334992.
Parks DJ, Blanchard SG, Bledsoe RK, et al. (1999). "Bile acids: natural ligands for an orphan nuclear receptor.". Science 284 (5418): 1365–8. PMID 10334993.
Bramlett KS, Yao S, Burris TP (2001). "Correlation of farnesoid X receptor coactivator recruitment and cholesterol 7alpha-hydroxylase gene repression by bile acids.". Mol. Genet. Metab. 71 (4): 609–15. doi:10.1006/mgme.2000.3106. PMID 11136553.
Stegh AH, Barnhart BC, Volkland J, et al. (2002). "Inactivation of caspase-8 on mitochondria of Bcl-xL-expressing MCF7-Fas cells: role for the bifunctional apoptosis regulator protein.". J. Biol. Chem. 277 (6): 4351–60. doi:10.1074/jbc.M108947200. PMID 11733517.
Cui J, Heard TS, Yu J, et al. (2002). "The amino acid residues asparagine 354 and isoleucine 372 of human farnesoid X receptor confer the receptor with high sensitivity to chenodeoxycholate.". J. Biol. Chem. 277 (29): 25963–9. doi:10.1074/jbc.M200824200. PMID 12004058.
Huber RM, Murphy K, Miao B, et al. (2002). "Generation of multiple farnesoid-X-receptor isoforms through the use of alternative promoters.". Gene 290 (1-2): 35–43. PMID 12062799.
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.
Pineda Torra I, Claudel T, Duval C, et al. (2003). "Bile acids induce the expression of the human peroxisome proliferator-activated receptor alpha gene via activation of the farnesoid X receptor.". Mol. Endocrinol. 17 (2): 259–72. PMID 12554753.
Anisfeld AM, Kast-Woelbern HR, Meyer ME, et al. (2003). "Syndecan-1 expression is regulated in an isoform-specific manner by the farnesoid-X receptor.". J. Biol. Chem. 278 (22): 20420–8. doi:10.1074/jbc.M302505200. PMID 12660231.
Pircher PC, Kitto JL, Petrowski ML, et al. (2003). "Farnesoid X receptor regulates bile acid-amino acid conjugation.". J. Biol. Chem. 278 (30): 27703–11. doi:10.1074/jbc.M302128200. PMID 12754200.
Zhao A, Lew JL, Huang L, et al. (2003). "Human kininogen gene is transactivated by the farnesoid X receptor.". J. Biol. Chem. 278 (31): 28765–70. doi:10.1074/jbc.M304568200. PMID 12761213.
Barbier O, Torra IP, Sirvent A, et al. (2003). "FXR induces the UGT2B4 enzyme in hepatocytes: a potential mechanism of negative feedback control of FXR activity.". Gastroenterology 124 (7): 1926–40. PMID 12806625.
Holt JA, Luo G, Billin AN, et al. (2003). "Definition of a novel growth factor-dependent signal cascade for the suppression of bile acid biosynthesis.". Genes Dev. 17 (13): 1581–91. doi:10.1101/gad.1083503. PMID 12815072.
Claudel T, Inoue Y, Barbier O, et al. (2003). "Farnesoid X receptor agonists suppress hepatic apolipoprotein CIII expression.". Gastroenterology 125 (2): 544–55. PMID 12891557.
Hsiao PW, Fryer CJ, Trotter KW, et al. (2003). "BAF60a mediates critical interactions between nuclear receptors and the BRG1 chromatin-remodeling complex for transactivation.". Mol. Cell. Biol. 23 (17): 6210–20. PMID 12917342.

[edit] External links

MeSH farnesoid+X-activated+receptor

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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)	AP-2

(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	HIVEP1

(2.5) Alternating composition	AIRE • DIDO1 • GRLF1 • ING (1, 2, 4) • JARID (1A, 1B, 1C, 1D, 2) • JMJD1B

(3) Helix-turn-helix
domains

(3.1) Homeo domain	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)

(3.3) Fork head / winged helix	E2F (1, 2, 3, 4, 5) • FOX proteins (C1, C2, E1, G1, H1, K2, L2, M1, N3, O1A, , O3A, O4, P1, P2, P3)

(3.4) Heat Shock Factors	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	p53

(4.4) MADS box	Mef2 (A, B, C, D) • SRF

(4.7) High mobility group	HNF (1A, 1B) • LEF1 • SOX (2, 3, 4, 5, 6, 8, 9, 10, 11, 13, 15, 18) • SRY • SSRP1

(4.10) Cold-shock domain	CSDA, YBX1

(4.11) Runt	CBF (CBFA2T2, CBFA2T3, RUNX1, RUNX2, RUNX3, RUNX1T1)

(0) Other
transcription factors

(0.2) HMGI(Y)	HMGA (1, 2) • HBP1

(0.3) Pocket domain	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

Categories: Genes on chromosome 12 | Human proteins | Biochemistry stubs | Intracellular receptors | Transcription factors

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Farnesoid X receptor

From Wikipedia, the free encyclopedia

[edit] References

[edit] Further reading

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