Biology:Nuclear receptor coactivator 2
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
The nuclear receptor coactivator 2 also known as NCoA-2 is a protein that in humans is encoded by the NCOA2 gene. NCoA-2 is also frequently called glucocorticoid receptor-interacting protein 1 (GRIP1), steroid receptor coactivator-2 (SRC-2), or transcriptional mediators/intermediary factor 2 (TIF2).
Function
NCoA-2 is a transcriptional coregulatory protein that contains several nuclear receptor interacting domains and an intrinsic histone acetyltransferase activity. NCOA2 is recruited to DNA promotion sites by ligand-activated nuclear receptors. NCOA2 in turn acetylates histones, which makes downstream DNA more accessible to transcription. Hence, NCOA2 assists nuclear receptors in the upregulation of DNA expression.[1][2]
GRIP1 is a transcriptional co-activator of the glucocorticoid receptor and interferon regulatory factor 1 (IRF1).[3]
Interactions
Nuclear receptor coactivator 2 has been shown to interact with:
- AR,[4][5][6][7][8]
- ARNT,[9]
- BRCA1,[10][11]
- DDX17,[12]
- DDX5,[12]
- ESR1,[7][12][13][14][15]
- NR3C1,[16][17]
- PPFIA4,[18]
- PPARG,[19]
- RXRA,[20][21]
- SRA1,[12] and
- VDR.[7][13][20][22]
References
- ↑ "TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors". EMBO J 15 (14): 3667–75. 1996. doi:10.1002/j.1460-2075.1996.tb00736.x. PMID 8670870.
- ↑ "GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors". Mol Cell Biol 17 (5): 2735–44. 1997. doi:10.1128/MCB.17.5.2735. PMID 9111344.
- ↑ "Glucocorticoid receptor interacting protein-1 restores glucocorticoid responsiveness in steroid-resistant airway structural cells". Am. J. Respir. Cell Mol. Biol. 42 (1): 9–15. January 2010. doi:10.1165/rcmb.2009-0239RC. PMID 19805480.
- ↑ "Antiandrogen effects of mifepristone on coactivator and corepressor interactions with the androgen receptor". Mol. Endocrinol. 18 (1): 70–85. 2004. doi:10.1210/me.2003-0189. PMID 14593076.
- ↑ "p54nrb acts as a transcriptional coactivator for activation function 1 of the human androgen receptor". Biochem. Biophys. Res. Commun. 306 (3): 660–5. 2003. doi:10.1016/S0006-291X(03)01021-0. PMID 12810069.
- ↑ "Mechanistic relationship between androgen receptor polyglutamine tract truncation and androgen-dependent transcriptional hyperactivity in prostate cancer cells". J. Biol. Chem. 279 (17): 17319–28. 2004. doi:10.1074/jbc.M400970200. PMID 14966121.
- ↑ 7.0 7.1 7.2 "Electrostatic modulation in steroid receptor recruitment of LXXLL and FXXLF motifs". Mol. Cell. Biol. 23 (6): 2135–50. 2003. doi:10.1128/MCB.23.6.2135-2150.2003. PMID 12612084.
- ↑ "Melanoma antigen gene protein MAGE-11 regulates androgen receptor function by modulating the interdomain interaction". Mol. Cell. Biol. 25 (4): 1238–57. 2005. doi:10.1128/MCB.25.4.1238-1257.2005. PMID 15684378.
- ↑ "Recruitment of the NCoA/SRC-1/p160 family of transcriptional coactivators by the aryl hydrocarbon receptor/aryl hydrocarbon receptor nuclear translocator complex". Mol. Cell. Biol. 22 (12): 4319–33. 2002. doi:10.1128/MCB.22.12.4319-4333.2002. PMID 12024042.
- ↑ "Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains". J. Biol. Chem. 278 (52): 52914–8. 2003. doi:10.1074/jbc.C300407200. PMID 14578343.
- ↑ "Breast cancer susceptibility gene 1 (BRCAI) is a coactivator of the androgen receptor". Cancer Res. 60 (21): 5946–9. 2000. PMID 11085509.
- ↑ 12.0 12.1 12.2 12.3 "A subfamily of RNA-binding DEAD-box proteins acts as an estrogen receptor alpha coactivator through the N-terminal activation domain (AF-1) with an RNA coactivator, SRA". EMBO J. 20 (6): 1341–52. 2001. doi:10.1093/emboj/20.6.1341. PMID 11250900.
- ↑ 13.0 13.1 "The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome". Cell 113 (7): 905–17. 2003. doi:10.1016/S0092-8674(03)00436-7. PMID 12837248.
- ↑ "Interaction of transcriptional intermediary factor 2 nuclear receptor box peptides with the coactivator binding site of estrogen receptor alpha". J. Biol. Chem. 277 (24): 21862–8. 2002. doi:10.1074/jbc.M200764200. PMID 11937504.
- ↑ "Recruitment of coactivator glucocorticoid receptor interacting protein 1 to an estrogen receptor transcription complex is regulated by the 3',5'-cyclic adenosine 5'-monophosphate-dependent protein kinase". Endocrinology 149 (9): 4336–45. 2008. doi:10.1210/en.2008-0037. PMID 18499756.
- ↑ "Regulation of glucocorticoid receptor activity by 14--3-3-dependent intracellular relocalization of the corepressor RIP140". Mol. Endocrinol. 15 (4): 501–11. 2001. doi:10.1210/mend.15.4.0624. PMID 11266503.
- ↑ "Crystal structure of the glucocorticoid receptor ligand binding domain reveals a novel mode of receptor dimerization and coactivator recognition". Cell 110 (1): 93–105. 2002. doi:10.1016/S0092-8674(02)00817-6. PMID 12151000.
- ↑ "Interaction between GRIP and liprin-alpha/SYD2 is required for AMPA receptor targeting". Neuron 34 (1): 39–52. 2002. doi:10.1016/S0896-6273(02)00640-2. PMID 11931740.
- ↑ "Ligand type-specific interactions of peroxisome proliferator-activated receptor gamma with transcriptional coactivators". J. Biol. Chem. 275 (43): 33201–4. 2000. doi:10.1074/jbc.C000517200. PMID 10944516.
- ↑ 20.0 20.1 "Ternary complexes and cooperative interplay between NCoA-62/Ski-interacting protein and steroid receptor coactivators in vitamin D receptor-mediated transcription". J. Biol. Chem. 276 (44): 40614–20. 2001. doi:10.1074/jbc.M106263200. PMID 11514567.
- ↑ "Interactions of RXR with coactivators are differentially mediated by helix 11 of the receptor's ligand binding domain". Biochemistry 41 (8): 2500–8. 2002. doi:10.1021/bi011764+. PMID 11851396.
- ↑ "Antagonistic action of a 25-carboxylic ester analogue of 1alpha, 25-dihydroxyvitamin D3 is mediated by a lack of ligand-induced vitamin D receptor interaction with coactivators". J. Biol. Chem. 275 (22): 16506–12. 2000. doi:10.1074/jbc.M910000199. PMID 10748178.
Further reading
- "TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors.". EMBO J. 15 (14): 3667–75. 1996. doi:10.1002/j.1460-2075.1996.tb00736.x. PMID 8670870.
- "GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors.". Mol. Cell. Biol. 17 (5): 2735–44. 1997. doi:10.1128/MCB.17.5.2735. PMID 9111344.
- "The coactivator TIF2 contains three nuclear receptor-binding motifs and mediates transactivation through CBP binding-dependent and -independent pathways.". EMBO J. 17 (2): 507–19. 1998. doi:10.1093/emboj/17.2.507. PMID 9430642.
- "A novel fusion between MOZ and the nuclear receptor coactivator TIF2 in acute myeloid leukemia.". Blood 91 (9): 3127–33. 1998. doi:10.1182/blood.V91.9.3127. PMID 9558366.
- "Chromatin remodelling by the glucocorticoid receptor requires the BRG1 complex.". Nature 393 (6680): 88–91. 1998. doi:10.1038/30032. PMID 9590696. Bibcode: 1998Natur.393...88F.
- "Functional interactions of the AF-2 activation domain core region of the human androgen receptor with the amino-terminal domain and with the transcriptional coactivator TIF2 (transcriptional intermediary factor2).". Mol. Endocrinol. 12 (8): 1172–83. 1998. doi:10.1210/mend.12.8.0153. PMID 9717843.
- "SRC-1 and GRIP1 coactivate transcription with hepatocyte nuclear factor 4.". J. Biol. Chem. 273 (47): 30847–50. 1998. doi:10.1074/jbc.273.47.30847. PMID 9812974.
- "An additional region of coactivator GRIP1 required for interaction with the hormone-binding domains of a subset of nuclear receptors.". J. Biol. Chem. 274 (6): 3496–502. 1999. doi:10.1074/jbc.274.6.3496. PMID 9920895.
- "Regulation of transcription by a protein methyltransferase.". Science 284 (5423): 2174–7. 1999. doi:10.1126/science.284.5423.2174. PMID 10381882.
- "Multiple signal input and output domains of the 160-kilodalton nuclear receptor coactivator proteins.". Mol. Cell. Biol. 19 (9): 6164–73. 1999. doi:10.1128/MCB.19.9.6164. PMID 10454563.
- "Coactivators for the orphan nuclear receptor RORalpha.". Mol. Endocrinol. 13 (9): 1550–7. 1999. doi:10.1210/mend.13.9.0343. PMID 10478845.
- "Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha.". Mol. Cell. Biol. 20 (1): 402–15. 2000. doi:10.1128/MCB.20.1.402-415.2000. PMID 10594042.
- "Constitutive activation of transcription and binding of coactivator by estrogen-related receptors 1 and 2.". Mol. Endocrinol. 13 (12): 2151–62. 2000. doi:10.1210/mend.13.12.0381. PMID 10598588.
- "Retinoic acid stimulation of the human surfactant protein B promoter is thyroid transcription factor 1 site-dependent.". J. Biol. Chem. 275 (1): 56–62. 2000. doi:10.1074/jbc.275.1.56. PMID 10617585.
- "Cloning of a mouse glucocorticoid modulatory element binding protein, a new member of the KDWK family.". FEBS Lett. 468 (2–3): 203–10. 2000. doi:10.1016/S0014-5793(00)01209-6. PMID 10692587.
- "Specific association of estrogen receptor beta with the cell cycle spindle assembly checkpoint protein, MAD2.". Proc. Natl. Acad. Sci. U.S.A. 97 (6): 2836–9. 2000. doi:10.1073/pnas.050580997. PMID 10706629. Bibcode: 2000PNAS...97.2836P.
- "Antagonistic action of a 25-carboxylic ester analogue of 1alpha, 25-dihydroxyvitamin D3 is mediated by a lack of ligand-induced vitamin D receptor interaction with coactivators.". J. Biol. Chem. 275 (22): 16506–12. 2000. doi:10.1074/jbc.M910000199. PMID 10748178.
- "Ligand type-specific interactions of peroxisome proliferator-activated receptor gamma with transcriptional coactivators.". J. Biol. Chem. 275 (43): 33201–4. 2000. doi:10.1074/jbc.C000517200. PMID 10944516.
- "Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities.". J. Biol. Chem. 276 (2): 1089–98. 2001. doi:10.1074/jbc.M004228200. PMID 11050077.
- "Breast cancer susceptibility gene 1 (BRCAI) is a coactivator of the androgen receptor.". Cancer Res. 60 (21): 5946–9. 2000. PMID 11085509.
External links
- nuclear receptor coactivator 2 at the US National Library of Medicine Medical Subject Headings (MeSH)
- NURSA C90
- Overview of all the structural information available in the PDB for UniProt: Q15596 (Human Nuclear receptor coactivator 2) at the PDBe-KB.
- Overview of all the structural information available in the PDB for UniProt: Q61026 (Mouse Nuclear receptor coactivator 2) at the PDBe-KB.
 |  |
