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Nuclear receptor coactivator 1

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The nuclear receptor coactivator 1 (NCOA1) is a transcriptional coregulatory protein that contains several nuclear receptor interacting domains and an intrinsic histone acetyltransferase activity (EC 2.3.1.48). NCOA1 is recruited to DNA promotion sites by ligand-activated nuclear receptors. NCOA1, in turn, acylates histones, which makes downsteam DNA more accessible to transcription. Hence, NCOA1 assists nuclear receptors in the upregulation of DNA expression.[1][2]

NCOA1 is also frequently called steroid receptor coactivator-1 (SRC-1).

Interactions

Nuclear receptor coactivator 1 possesses a basic helix-loop-helix (bHLH) domain and has been shown to interact with:

References

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  2. ^ Onate SA, Boonyaratanakornkit V, Spencer TE, Tsai SY, Tsai MJ, Edwards DP, O'Malley BW (1998). "The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors". J Biol Chem. 273 (20): 12101–8. doi:10.1074/jbc.273.20.12101. PMID 9575154.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  3. ^ Masiello D, Chen SY, Xu Y, Verhoeven MC, Choi E, Hollenberg AN, Balk SP (Oct 2004). "Recruitment of beta-catenin by wild-type or mutant androgen receptors correlates with ligand-stimulated growth of prostate cancer cells". Mol. Endocrinol. 18 (10): 2388–401. doi:10.1210/me.2003-0436. PMID 15256534.
  4. ^ Ueda T, Mawji NR, Bruchovsky N, Sadar MD (Oct 2002). "Ligand-independent activation of the androgen receptor by interleukin-6 and the role of steroid receptor coactivator-1 in prostate cancer cells". J. Biol. Chem. 277 (41): 38087–94. doi:10.1074/jbc.M203313200. PMID 12163482.{{cite journal}}: CS1 maint: unflagged free DOI (link)
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  12. ^ Zwijsen RM, Buckle RS, Hijmans EM, Loomans CJ, Bernards R (Nov 1998). "Ligand-independent recruitment of steroid receptor coactivators to estrogen receptor by cyclin D1". Genes Dev. 12 (22): 3488–98. doi:10.1101/gad.12.22.3488. PMC 317237. PMID 9832502.
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  15. ^ Kalkhoven E, Valentine JE, Heery DM, Parker MG (Jan 1998). "Isoforms of steroid receptor co-activator 1 differ in their ability to potentiate transcription by the oestrogen receptor". EMBO J. 17 (1): 232–43. doi:10.1093/emboj/17.1.232. PMC 1170374. PMID 9427757.
  16. ^ Kang YK, Guermah M, Yuan CX, Roeder RG (Mar 2002). "The TRAP/Mediator coactivator complex interacts directly with estrogen receptors alpha and beta through the TRAP220 subunit and directly enhances estrogen receptor function in vitro". Proc. Natl. Acad. Sci. U.S.A. 99 (5): 2642–7. doi:10.1073/pnas.261715899. PMC 122401. PMID 11867769.
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  18. ^ Kucera T, Waltner-Law M, Scott DK, Prasad R, Granner DK (Jul 2002). "A point mutation of the AF2 transactivation domain of the glucocorticoid receptor disrupts its interaction with steroid receptor coactivator 1". J. Biol. Chem. 277 (29): 26098–102. doi:10.1074/jbc.M204013200. PMID 12118039.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  19. ^ Na SY, Lee SK, Han SJ, Choi HS, Im SY, Lee JW (May 1998). "Steroid receptor coactivator-1 interacts with the p50 subunit and coactivates nuclear factor kappaB-mediated transactivations". J. Biol. Chem. 273 (18): 10831–4. doi:10.1074/jbc.273.18.10831. PMID 9556555.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  20. ^ Spencer TE, Jenster G, Burcin MM, Allis CD, Zhou J, Mizzen CA, McKenna NJ, Onate SA, Tsai SY, Tsai MJ, O'Malley BW (Sep 1997). "Steroid receptor coactivator-1 is a histone acetyltransferase". Nature. 389 (6647): 194–8. doi:10.1038/38304. PMID 9296499.
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  24. ^ Zhang C, Baudino TA, Dowd DR, Tokumaru H, Wang W, MacDonald PN (Nov 2001). "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. doi:10.1074/jbc.M106263200. PMID 11514567.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  25. ^ Giraud S, Bienvenu F, Avril S, Gascan H, Heery DM, Coqueret O (Mar 2002). "Functional interaction of STAT3 transcription factor with the coactivator NcoA/SRC1a". J. Biol. Chem. 277 (10): 8004–11. doi:10.1074/jbc.M111486200. PMID 11773079.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  26. ^ Litterst CM, Pfitzner E (Dec 2001). "Transcriptional activation by STAT6 requires the direct interaction with NCoA-1". J. Biol. Chem. 276 (49): 45713–21. doi:10.1074/jbc.M108132200. PMID 11574547.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  27. ^ Litterst CM, Pfitzner E (Sep 2002). "An LXXLL motif in the transactivation domain of STAT6 mediates recruitment of NCoA-1/SRC-1". J. Biol. Chem. 277 (39): 36052–60. doi:10.1074/jbc.M203556200. PMID 12138096.{{cite journal}}: CS1 maint: unflagged free DOI (link)
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  29. ^ Liu Y, Takeshita A, Misiti S, Chin WW, Yen PM (Oct 1998). "Lack of coactivator interaction can be a mechanism for dominant negative activity by mutant thyroid hormone receptors". Endocrinology. 139 (10): 4197–204. doi:10.1210/endo.139.10.6218. PMID 9751500.
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Further reading

  • Qi C, Zhu Y, Reddy JK (2001). "Peroxisome proliferator-activated receptors, coactivators, and downstream targets". Cell Biochem. Biophys. 32. Spring: 187–204. PMID 11330046.