메뉴 건너뛰기




Volumn 384, Issue 3, 2009, Pages 389-393

Molecular determinants of the interactions between LXR/RXR heterodimers and TRAP220

Author keywords

Allosteric activation; Liver X receptor; LXR RXR heterodimers; NR box (LXXLL motif); NR specificity; One plus two hybrid system; TRAP220 coactivator

Indexed keywords

CELL NUCLEUS RECEPTOR; FURYLFURAMIDE; HETERODIMER; LIVER X RECEPTOR; PROLINE; PROTEIN; RETINOID X RECEPTOR; TRAP220 PROTEIN; UNCLASSIFIED DRUG;

EID: 65649131624     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.04.131     Document Type: Article
Times cited : (13)

References (25)
  • 1
    • 33646204900 scopus 로고    scopus 로고
    • A novel principle for partial agonism of liver X receptor ligands. Competitive recruitment of activators and repressors
    • Albers M., Blume B., Schlueter T., Wright M.B., Kober I., Kremoser C., Deuschle U., and Koegl M. A novel principle for partial agonism of liver X receptor ligands. Competitive recruitment of activators and repressors. J. Biol. Chem. 281 (2006) 4920-4930
    • (2006) J. Biol. Chem. , vol.281 , pp. 4920-4930
    • Albers, M.1    Blume, B.2    Schlueter, T.3    Wright, M.B.4    Kober, I.5    Kremoser, C.6    Deuschle, U.7    Koegl, M.8
  • 2
    • 0030986236 scopus 로고    scopus 로고
    • A signature motif in transcriptional co-activators mediates binding to nuclear receptors
    • Heery D.M., Kalkhoven E., Hoare S., and Parker M.G. A signature motif in transcriptional co-activators mediates binding to nuclear receptors. Nature 387 (1997) 733-736
    • (1997) Nature , vol.387 , pp. 733-736
    • Heery, D.M.1    Kalkhoven, E.2    Hoare, S.3    Parker, M.G.4
  • 3
    • 33644651160 scopus 로고    scopus 로고
    • Liver X receptors as integrators of metabolic and inflammatory signaling
    • Zelcer N., and Tontonoz P. Liver X receptors as integrators of metabolic and inflammatory signaling. J. Clin. Invest. 116 (2006) 607-614
    • (2006) J. Clin. Invest. , vol.116 , pp. 607-614
    • Zelcer, N.1    Tontonoz, P.2
  • 4
    • 0031011661 scopus 로고    scopus 로고
    • Heterodimeric interaction between retinoid X receptor alpha and orphan nuclear receptor OR1 reveals dimerization-induced activation as a novel mechanism of nuclear receptor activation
    • Wiebel F.F., and Gustafsson J.A. Heterodimeric interaction between retinoid X receptor alpha and orphan nuclear receptor OR1 reveals dimerization-induced activation as a novel mechanism of nuclear receptor activation. Mol. Cell. Biol. 17 (1997) 3977-3986
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3977-3986
    • Wiebel, F.F.1    Gustafsson, J.A.2
  • 5
    • 0033326582 scopus 로고    scopus 로고
    • Ligand-independent coregulator recruitment by the triply activatable OR1/retinoid X receptor-alpha nuclear receptor heterodimer
    • Wiebel F.F., Steffensen K.R., Treuter E., Feltkamp D., and Gustafsson J.A. Ligand-independent coregulator recruitment by the triply activatable OR1/retinoid X receptor-alpha nuclear receptor heterodimer. Mol. Endocrinol. 13 (1999) 1105-1118
    • (1999) Mol. Endocrinol. , vol.13 , pp. 1105-1118
    • Wiebel, F.F.1    Steffensen, K.R.2    Treuter, E.3    Feltkamp, D.4    Gustafsson, J.A.5
  • 11
    • 0037841590 scopus 로고    scopus 로고
    • Role of the LXXLL-motif and activation function 2 domain in subcellular localization of Dax-1 (dosage-sensitive sex reversal-adrenal hypoplasia-congenita critical region on the X chromosome, gene 1)
    • Kawajiri K., Ikuta T., Suzuki T., Kusaka M., Muramatsu M., Fujieda K., Tachibana M., and Morohashi K. Role of the LXXLL-motif and activation function 2 domain in subcellular localization of Dax-1 (dosage-sensitive sex reversal-adrenal hypoplasia-congenita critical region on the X chromosome, gene 1). Mol. Endocrinol. 17 (2003) 994-1004
    • (2003) Mol. Endocrinol. , vol.17 , pp. 994-1004
    • Kawajiri, K.1    Ikuta, T.2    Suzuki, T.3    Kusaka, M.4    Muramatsu, M.5    Fujieda, K.6    Tachibana, M.7    Morohashi, K.8
  • 12
    • 0141481039 scopus 로고    scopus 로고
    • Induction of intestinal ATP-binding cassette transporters by a phytosterol-derived liver X receptor agonist
    • Kaneko E., Matsuda M., Yamada Y., Tachibana Y., Shimomura I., and Makishima M. Induction of intestinal ATP-binding cassette transporters by a phytosterol-derived liver X receptor agonist. J. Biol. Chem. 278 (2003) 36091-36098
    • (2003) J. Biol. Chem. , vol.278 , pp. 36091-36098
    • Kaneko, E.1    Matsuda, M.2    Yamada, Y.3    Tachibana, Y.4    Shimomura, I.5    Makishima, M.6
  • 13
    • 40449093255 scopus 로고    scopus 로고
    • RXR heterodimerization allosterically activates LXR binding to the second NR box of activating signal co-integrator-2
    • Son Y.L., Park O.G., Kim G.S., Lee J.W., and Lee Y.C. RXR heterodimerization allosterically activates LXR binding to the second NR box of activating signal co-integrator-2. Biochem. J. 410 (2008) 319-330
    • (2008) Biochem. J. , vol.410 , pp. 319-330
    • Son, Y.L.1    Park, O.G.2    Kim, G.S.3    Lee, J.W.4    Lee, Y.C.5
  • 14
    • 0035318741 scopus 로고    scopus 로고
    • The TRAP/SMCC/Mediator complex and thyroid hormone receptor function
    • Ito M., and Roeder R.G. The TRAP/SMCC/Mediator complex and thyroid hormone receptor function. Trends Endocrinol. Metab. 12 (2001) 127-134
    • (2001) Trends Endocrinol. Metab. , vol.12 , pp. 127-134
    • Ito, M.1    Roeder, R.G.2
  • 15
    • 0033928379 scopus 로고    scopus 로고
    • Specific structural motifs determine TRAP220 interactions with nuclear hormone receptors
    • Ren Y., Behre E., Ren Z., Zhang J., Wang Q., and Fondell J.D. Specific structural motifs determine TRAP220 interactions with nuclear hormone receptors. Mol. Cell. Biol. 20 (2000) 5433-5446
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5433-5446
    • Ren, Y.1    Behre, E.2    Ren, Z.3    Zhang, J.4    Wang, Q.5    Fondell, J.D.6
  • 16
    • 35648977580 scopus 로고    scopus 로고
    • One- plus two-hybrid system, a novel yeast genetic selection for specific missense mutations disrupting protein/protein interactions
    • Kim J.Y., Park O.G., Lee J.W., and Lee Y.C. One- plus two-hybrid system, a novel yeast genetic selection for specific missense mutations disrupting protein/protein interactions. Mol. Cell. Proteomics 6 (2007) 1727-1740
    • (2007) Mol. Cell. Proteomics , vol.6 , pp. 1727-1740
    • Kim, J.Y.1    Park, O.G.2    Lee, J.W.3    Lee, Y.C.4
  • 17
    • 0033201447 scopus 로고    scopus 로고
    • Bcl3, an IkappaB protein, stimulates activating protein-1 transactivation and cellular proliferation
    • Na S.Y., Choi J.E., Kim H.J., Jhun B.H., Lee Y.C., and Lee J.W. Bcl3, an IkappaB protein, stimulates activating protein-1 transactivation and cellular proliferation. J. Biol. Chem. 274 (1999) 28491-28496
    • (1999) J. Biol. Chem. , vol.274 , pp. 28491-28496
    • Na, S.Y.1    Choi, J.E.2    Kim, H.J.3    Jhun, B.H.4    Lee, Y.C.5    Lee, J.W.6
  • 19
    • 0038514176 scopus 로고    scopus 로고
    • An extended LXXLL motif sequence determines the nuclear receptor binding specificity of TRAP220
    • Coulthard V.H., Matsuda S., and Heery D.M. An extended LXXLL motif sequence determines the nuclear receptor binding specificity of TRAP220. J. Biol. Chem. 278 (2003) 10942-10951
    • (2003) J. Biol. Chem. , vol.278 , pp. 10942-10951
    • Coulthard, V.H.1    Matsuda, S.2    Heery, D.M.3
  • 20
    • 0034034013 scopus 로고    scopus 로고
    • The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes
    • Rachez C., Gamble M., Chang C.P., Atkins G.B., Lazar M.A., and Freedman L.P. The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes. Mol. Cell. Biol. 20 (2000) 2718-2726
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 2718-2726
    • Rachez, C.1    Gamble, M.2    Chang, C.P.3    Atkins, G.B.4    Lazar, M.A.5    Freedman, L.P.6
  • 22
    • 19944430311 scopus 로고    scopus 로고
    • Characterization of the interaction between retinoic acid receptor/retinoid X receptor (RAR/RXR) heterodimers and transcriptional coactivators through structural and fluorescence anisotropy studies
    • Pogenberg V., Guichou J.F., Vivat-Hannah V., Kammerer S., Perez E., Germain P., de Lera A.R., Gronemeyer H., Royer C.A., and Bourguet W. Characterization of the interaction between retinoic acid receptor/retinoid X receptor (RAR/RXR) heterodimers and transcriptional coactivators through structural and fluorescence anisotropy studies. J. Biol. Chem. 280 (2005) 1625-1633
    • (2005) J. Biol. Chem. , vol.280 , pp. 1625-1633
    • Pogenberg, V.1    Guichou, J.F.2    Vivat-Hannah, V.3    Kammerer, S.4    Perez, E.5    Germain, P.6    de Lera, A.R.7    Gronemeyer, H.8    Royer, C.A.9    Bourguet, W.10
  • 25
    • 0033513582 scopus 로고    scopus 로고
    • Dissection of the LXXLL nuclear receptor-coactivator interaction motif using combinatorial peptide libraries: discovery of peptide antagonists of estrogen receptors alpha and beta
    • Chang C., Norris J.D., Gron H., Paige L.A., Hamilton P.T., Kenan D.J., Fowlkes D., and McDonnell D.P. Dissection of the LXXLL nuclear receptor-coactivator interaction motif using combinatorial peptide libraries: discovery of peptide antagonists of estrogen receptors alpha and beta. Mol. Cell. Biol. 19 (1999) 8226-8239
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 8226-8239
    • Chang, C.1    Norris, J.D.2    Gron, H.3    Paige, L.A.4    Hamilton, P.T.5    Kenan, D.J.6    Fowlkes, D.7    McDonnell, D.P.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.