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Volumn 1851, Issue 1, 2015, Pages 66-75

Retinoic acid signaling and mouse embryonic stem cell differentiation: Cross talk between genomic and non-genomic effects of RA

Author keywords

Embryonic stem cell; Nuclear receptor; Phosphorylation; Retinoic acid; Transcription

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; RETINOIC ACID; RETINOIC ACID RECEPTOR; RETINOIC ACID RECEPTOR GAMMA; SERINE;

EID: 84911470944     PISSN: 13881981     EISSN: 18792618     Source Type: Journal    
DOI: 10.1016/j.bbalip.2014.04.003     Document Type: Review
Times cited : (87)

References (79)
  • 1
    • 79953722853 scopus 로고    scopus 로고
    • Vitamin A in reproduction and development
    • M. Clagett-Dame, and D. Knutson Vitamin A in reproduction and development Nutrients 3 2011 385 428
    • (2011) Nutrients , vol.3 , pp. 385-428
    • Clagett-Dame, M.1    Knutson, D.2
  • 2
    • 83255185195 scopus 로고    scopus 로고
    • Signaling by vitamin A and retinol-binding protein in regulation of insulin responses and lipid homeostasis
    • D.C. Berry, and N. Noy Signaling by vitamin A and retinol-binding protein in regulation of insulin responses and lipid homeostasis Biochim. Biophys. Acta 1821 2012 168 176
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 168-176
    • Berry, D.C.1    Noy, N.2
  • 3
    • 83255185264 scopus 로고    scopus 로고
    • Lipid metabolism in mammalian tissues and its control by retinoic acid
    • M.L. Bonet, J. Ribot, and A. Palou Lipid metabolism in mammalian tissues and its control by retinoic acid Biochim. Biophys. Acta 1821 2012 177 189
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 177-189
    • Bonet, M.L.1    Ribot, J.2    Palou, A.3
  • 4
    • 83255192152 scopus 로고    scopus 로고
    • Retinoid chemistry: Synthesis and application for metabolic disease
    • R.W. Curley Jr. Retinoid chemistry: synthesis and application for metabolic disease Biochim. Biophys. Acta 1821 2012 3 9
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 3-9
    • Curley, R.W.1
  • 5
    • 0034660094 scopus 로고    scopus 로고
    • Retinoid-binding proteins: Mediators of retinoid action
    • N. Noy Retinoid-binding proteins: mediators of retinoid action Biochem. J. 348 Pt 3 2000 481 495
    • (2000) Biochem. J. , vol.348 , pp. 481-495
    • Noy, N.1
  • 7
    • 0036203716 scopus 로고    scopus 로고
    • Direct channeling of retinoic acid between cellular retinoic acid-binding protein II and retinoic acid receptor sensitizes mammary carcinoma cells to retinoic acid-induced growth arrest
    • A.S. Budhu, and N. Noy Direct channeling of retinoic acid between cellular retinoic acid-binding protein II and retinoic acid receptor sensitizes mammary carcinoma cells to retinoic acid-induced growth arrest Mol. Cell. Biol. 22 2002 2632 2641
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2632-2641
    • Budhu, A.S.1    Noy, N.2
  • 8
    • 0032875365 scopus 로고    scopus 로고
    • Physical and functional interactions between cellular retinoic acid binding protein II and the retinoic acid-dependent nuclear complex
    • L. Delva, J.N. Bastie, C. Rochette-Egly, R. Kraiba, N. Balitrand, G. Despouy, P. Chambon, and C. Chomienne Physical and functional interactions between cellular retinoic acid binding protein II and the retinoic acid-dependent nuclear complex Mol. Cell. Biol. 19 1999 7158 7167
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7158-7167
    • Delva, L.1    Bastie, J.N.2    Rochette-Egly, C.3    Kraiba, R.4    Balitrand, N.5    Despouy, G.6    Chambon, P.7    Chomienne, C.8
  • 9
    • 82655180888 scopus 로고    scopus 로고
    • Nuclear retinoic acid receptors: Conductors of the retinoic acid symphony during development
    • E. Samarut, and C. Rochette-Egly Nuclear retinoic acid receptors: conductors of the retinoic acid symphony during development Mol. Cell. Endocrinol. 348 2012 348 360
    • (2012) Mol. Cell. Endocrinol. , vol.348 , pp. 348-360
    • Samarut, E.1    Rochette-Egly, C.2
  • 10
    • 84878977179 scopus 로고    scopus 로고
    • Vitamin A and retinoid signaling: Genomic and nongenomic effects: Thematic review series: Fat-soluble vitamins: Vitamin A
    • Z. Al Tanoury, A. Piskunov, and C. Rochette-Egly Vitamin A and retinoid signaling: genomic and nongenomic effects: thematic review series: fat-soluble vitamins: vitamin A J. Lipid Res. 54 2013 1761 1775
    • (2013) J. Lipid Res. , vol.54 , pp. 1761-1775
    • Al Tanoury, Z.1    Piskunov, A.2    Rochette-Egly, C.3
  • 11
    • 0034698181 scopus 로고    scopus 로고
    • TFIIH interacts with the retinoic acid receptor gamma and phosphorylates its AF-1-activating domain through cdk7
    • J. Bastien, S. Adam-Stitah, T. Riedl, J.M. Egly, P. Chambon, and C. Rochette-Egly TFIIH interacts with the retinoic acid receptor gamma and phosphorylates its AF-1-activating domain through cdk7 J. Biol. Chem. 275 2000 21896 21904
    • (2000) J. Biol. Chem. , vol.275 , pp. 21896-21904
    • Bastien, J.1    Adam-Stitah, S.2    Riedl, T.3    Egly, J.M.4    Chambon, P.5    Rochette-Egly, C.6
  • 12
    • 0031440878 scopus 로고    scopus 로고
    • Stimulation of RAR alpha activation function AF-1 through binding to the general transcription factor TFIIH and phosphorylation by CDK7
    • C. Rochette-Egly, S. Adam, M. Rossignol, J.M. Egly, and P. Chambon Stimulation of RAR alpha activation function AF-1 through binding to the general transcription factor TFIIH and phosphorylation by CDK7 Cell 90 1997 97 107
    • (1997) Cell , vol.90 , pp. 97-107
    • Rochette-Egly, C.1    Adam, S.2    Rossignol, M.3    Egly, J.M.4    Chambon, P.5
  • 14
    • 0029794132 scopus 로고    scopus 로고
    • A decade of molecular biology of retinoic acid receptors
    • P. Chambon A decade of molecular biology of retinoic acid receptors FASEB J. 10 1996 940 954
    • (1996) FASEB J. , vol.10 , pp. 940-954
    • Chambon, P.1
  • 15
    • 68049143179 scopus 로고    scopus 로고
    • Dynamic and combinatorial control of gene expression by nuclear retinoic acid receptors
    • C. Rochette-Egly, and P. Germain Dynamic and combinatorial control of gene expression by nuclear retinoic acid receptors Nucl. Recept. Signal. 7 2009 e005
    • (2009) Nucl. Recept. Signal. , vol.7 , pp. 005
    • Rochette-Egly, C.1    Germain, P.2
  • 16
    • 1542710344 scopus 로고    scopus 로고
    • Nuclear retinoid receptors and the transcription of retinoid-target genes
    • J. Bastien, and C. Rochette-Egly Nuclear retinoid receptors and the transcription of retinoid-target genes Gene 328 2004 1 16
    • (2004) Gene , vol.328 , pp. 1-16
    • Bastien, J.1    Rochette-Egly, C.2
  • 17
    • 0034306499 scopus 로고    scopus 로고
    • Nuclear receptor ligand-binding domains: Three-dimensional structures, molecular interactions and pharmacological implications
    • W. Bourguet, P. Germain, and H. Gronemeyer Nuclear receptor ligand-binding domains: three-dimensional structures, molecular interactions and pharmacological implications Trends Pharmacol. Sci. 21 2000 381 388
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 381-388
    • Bourguet, W.1    Germain, P.2    Gronemeyer, H.3
  • 18
    • 34848862778 scopus 로고    scopus 로고
    • Design of selective nuclear receptor modulators: RAR and RXR as a case study
    • A.R. de Lera, W. Bourguet, L. Altucci, and H. Gronemeyer Design of selective nuclear receptor modulators: RAR and RXR as a case study Nat. Rev. Drug Discov. 6 2007 811 820
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 811-820
    • De Lera, A.R.1    Bourguet, W.2    Altucci, L.3    Gronemeyer, H.4
  • 19
    • 34249751092 scopus 로고    scopus 로고
    • Protein kinases and the proteasome join in the combinatorial control of transcription by nuclear retinoic acid receptors
    • G. Bour, S. Lalevee, and C. Rochette-Egly Protein kinases and the proteasome join in the combinatorial control of transcription by nuclear retinoic acid receptors Trends Cell Biol. 17 2007 302 309
    • (2007) Trends Cell Biol. , vol.17 , pp. 302-309
    • Bour, G.1    Lalevee, S.2    Rochette-Egly, C.3
  • 20
    • 79959425215 scopus 로고    scopus 로고
    • Evolution of nuclear retinoic acid receptors alpha (RARa) phosphorylation sites. Serine gain provides fine-tuned regulation
    • E. Samarut, I. Amal, G. Markov, R. Stote, A. Dejaegere, V. Laudet, and C. Rochette-Egly Evolution of nuclear retinoic acid receptors alpha (RARa) phosphorylation sites. Serine gain provides fine-tuned regulation. Mol. Biol. Evol. 28 2011 2125 2137
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2125-2137
    • Samarut, E.1    Amal, I.2    Markov, G.3    Stote, R.4    Dejaegere, A.5    Laudet, V.6    Rochette-Egly, C.7
  • 23
    • 0035962669 scopus 로고    scopus 로고
    • Nuclear receptors coordinate the activities of chromatin remodeling complexes and coactivators to facilitate initiation of transcription
    • F.J. Dilworth, and P. Chambon Nuclear receptors coordinate the activities of chromatin remodeling complexes and coactivators to facilitate initiation of transcription Oncogene 20 2001 3047 3054
    • (2001) Oncogene , vol.20 , pp. 3047-3054
    • Dilworth, F.J.1    Chambon, P.2
  • 24
    • 75649135910 scopus 로고    scopus 로고
    • Deconstructing repression: Evolving models of co-repressor action
    • V. Perissi, K. Jepsen, C.K. Glass, and M.G. Rosenfeld Deconstructing repression: evolving models of co-repressor action Nat. Rev. Genet. 11 2010 109 123
    • (2010) Nat. Rev. Genet. , vol.11 , pp. 109-123
    • Perissi, V.1    Jepsen, K.2    Glass, C.K.3    Rosenfeld, M.G.4
  • 25
    • 78649646015 scopus 로고    scopus 로고
    • Retinoids regulate stem cell differentiation
    • L.J. Gudas, and J.A. Wagner Retinoids regulate stem cell differentiation J. Cell. Physiol. 226 2011 322 330
    • (2011) J. Cell. Physiol. , vol.226 , pp. 322-330
    • Gudas, L.J.1    Wagner, J.A.2
  • 26
    • 79952811257 scopus 로고    scopus 로고
    • Epigenomic reorganization of the clustered Hox genes in embryonic stem cells induced by retinoic acid
    • V. Kashyap, L.J. Gudas, F. Brenet, P. Funk, A. Viale, and J.M. Scandura Epigenomic reorganization of the clustered Hox genes in embryonic stem cells induced by retinoic acid J. Biol. Chem. 286 2011 3250 3260
    • (2011) J. Biol. Chem. , vol.286 , pp. 3250-3260
    • Kashyap, V.1    Gudas, L.J.2    Brenet, F.3    Funk, P.4    Viale, A.5    Scandura, J.M.6
  • 28
    • 0034650893 scopus 로고    scopus 로고
    • The coregulator exchange in transcriptional functions of nuclear receptors
    • C.K. Glass, and M.G. Rosenfeld The coregulator exchange in transcriptional functions of nuclear receptors Genes Dev. 14 2000 121 141
    • (2000) Genes Dev. , vol.14 , pp. 121-141
    • Glass, C.K.1    Rosenfeld, M.G.2
  • 30
    • 36348993236 scopus 로고    scopus 로고
    • Retinoic acid receptor isotype specificity in F9 teratocarcinoma stem cells results from the differential recruitment of coregulators to retinoic response elements
    • R.F. Gillespie, and L.J. Gudas Retinoic acid receptor isotype specificity in F9 teratocarcinoma stem cells results from the differential recruitment of coregulators to retinoic response elements J. Biol. Chem. 282 2007 33421 33434
    • (2007) J. Biol. Chem. , vol.282 , pp. 33421-33434
    • Gillespie, R.F.1    Gudas, L.J.2
  • 31
    • 34547941825 scopus 로고    scopus 로고
    • Retinoid regulated association of transcriptional co-regulators and the polycomb group protein SUZ12 with the retinoic acid response elements of Hoxa1, RARbeta(2), and Cyp26A1 in F9 embryonal carcinoma cells
    • R.F. Gillespie, and L.J. Gudas Retinoid regulated association of transcriptional co-regulators and the polycomb group protein SUZ12 with the retinoic acid response elements of Hoxa1, RARbeta(2), and Cyp26A1 in F9 embryonal carcinoma cells J. Mol. Biol. 372 2007 298 316
    • (2007) J. Mol. Biol. , vol.372 , pp. 298-316
    • Gillespie, R.F.1    Gudas, L.J.2
  • 32
    • 77951992661 scopus 로고    scopus 로고
    • Epigenetic regulatory mechanisms distinguish retinoic acid-mediated transcriptional responses in stem cells and fibroblasts
    • V. Kashyap, and L.J. Gudas Epigenetic regulatory mechanisms distinguish retinoic acid-mediated transcriptional responses in stem cells and fibroblasts J. Biol. Chem. 285 2010 14534 14548
    • (2010) J. Biol. Chem. , vol.285 , pp. 14534-14548
    • Kashyap, V.1    Gudas, L.J.2
  • 33
    • 33744792310 scopus 로고    scopus 로고
    • Sensors and signals: A coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response
    • M.G. Rosenfeld, V.V. Lunyak, and C.K. Glass Sensors and signals: a coactivator/corepressor/epigenetic code for integrating signal-dependent programs of transcriptional response Genes Dev. 20 2006 1405 1428
    • (2006) Genes Dev. , vol.20 , pp. 1405-1428
    • Rosenfeld, M.G.1    Lunyak, V.V.2    Glass, C.K.3
  • 34
    • 80054088836 scopus 로고    scopus 로고
    • Dissecting the retinoid-induced differentiation of F9 embryonal stem cells by integrative genomics
    • M.A. Mendoza-Parra, M. Walia, M. Sankar, and H. Gronemeyer Dissecting the retinoid-induced differentiation of F9 embryonal stem cells by integrative genomics Mol. Syst. Biol. 7 2011 538
    • (2011) Mol. Syst. Biol. , vol.7 , pp. 538
    • Mendoza-Parra, M.A.1    Walia, M.2    Sankar, M.3    Gronemeyer, H.4
  • 35
    • 58149354155 scopus 로고    scopus 로고
    • A coordinated phosphorylation cascade initiated by p38MAPK/MSK1 directs RARalpha to target promoters
    • N. Bruck, D. Vitoux, C. Ferry, V. Duong, A. Bauer, H. de The, and C. Rochette-Egly A coordinated phosphorylation cascade initiated by p38MAPK/MSK1 directs RARalpha to target promoters EMBO J. 28 2009 34 47
    • (2009) EMBO J. , vol.28 , pp. 34-47
    • Bruck, N.1    Vitoux, D.2    Ferry, C.3    Duong, V.4    Bauer, A.5    De The, H.6    Rochette-Egly, C.7
  • 37
    • 0037099584 scopus 로고    scopus 로고
    • Phosphorylation by p38MAPK and recruitment of SUG-1 are required for RA-indced RARγ degradation and transactivation
    • M. Gianni, A. Bauer, E. Garattini, P. Chambon, and C. Rochette-Egly Phosphorylation by p38MAPK and recruitment of SUG-1 are required for RA-indced RARγ degradation and transactivation EMBO J. 21 2002 3760 3769
    • (2002) EMBO J. , vol.21 , pp. 3760-3769
    • Gianni, M.1    Bauer, A.2    Garattini, E.3    Chambon, P.4    Rochette-Egly, C.5
  • 38
    • 84863786925 scopus 로고    scopus 로고
    • A retinoic acid receptor RARalpha pool present in membrane lipid rafts forms complexes with G protein alphaQ to activate p38MAPK
    • A. Piskunov, and C. Rochette-Egly A retinoic acid receptor RARalpha pool present in membrane lipid rafts forms complexes with G protein alphaQ to activate p38MAPK Oncogene 31 2012 3333 3345
    • (2012) Oncogene , vol.31 , pp. 3333-3345
    • Piskunov, A.1    Rochette-Egly, C.2
  • 39
    • 38049162240 scopus 로고    scopus 로고
    • All-trans-retinoic acid stimulates translation and induces spine formation in hippocampal neurons through a membrane-associated RARalpha
    • N. Chen, and J.L. Napoli All-trans-retinoic acid stimulates translation and induces spine formation in hippocampal neurons through a membrane-associated RARalpha FASEB J. 22 2008 236 245
    • (2008) FASEB J. , vol.22 , pp. 236-245
    • Chen, N.1    Napoli, J.L.2
  • 40
    • 34347394194 scopus 로고    scopus 로고
    • CSK controls retinoic acid receptor (RAR) signaling: A RAR-c-SRC signaling axis is required for neuritogenic differentiation
    • N. Dey, P.K. De, M. Wang, H. Zhang, E.A. Dobrota, K.A. Robertson, and D.L. Durden CSK controls retinoic acid receptor (RAR) signaling: a RAR-c-SRC signaling axis is required for neuritogenic differentiation Mol. Cell. Biol. 27 2007 4179 4197
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 4179-4197
    • Dey, N.1    De, P.K.2    Wang, M.3    Zhang, H.4    Dobrota, E.A.5    Robertson, K.A.6    Durden, D.L.7
  • 41
    • 49649090416 scopus 로고    scopus 로고
    • Retinoic acid-stimulated sequential phosphorylation, PML recruitment, and SUMOylation of nuclear receptor TR2 to suppress Oct4 expression
    • P. Gupta, P.C. Ho, M.M. Huq, S.G. Ha, S.W. Park, A.A. Khan, N.P. Tsai, and L.N. Wei Retinoic acid-stimulated sequential phosphorylation, PML recruitment, and SUMOylation of nuclear receptor TR2 to suppress Oct4 expression Proc. Natl. Acad. Sci. U. S. A. 105 2008 11424 11429
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 11424-11429
    • Gupta, P.1    Ho, P.C.2    Huq, M.M.3    Ha, S.G.4    Park, S.W.5    Khan, A.A.6    Tsai, N.P.7    Wei, L.N.8
  • 42
    • 34948828965 scopus 로고    scopus 로고
    • Rapid, nongenomic actions of retinoic acid on phosphatidylinositol-3-kinase signaling pathway mediated by the retinoic acid receptor
    • S. Masia, S. Alvarez, A.R. de Lera, and D. Barettino Rapid, nongenomic actions of retinoic acid on phosphatidylinositol-3-kinase signaling pathway mediated by the retinoic acid receptor Mol. Endocrinol. 21 2007 2391 2402
    • (2007) Mol. Endocrinol. , vol.21 , pp. 2391-2402
    • Masia, S.1    Alvarez, S.2    De Lera, A.R.3    Barettino, D.4
  • 43
    • 84867584796 scopus 로고    scopus 로고
    • Cellular retinoic acid binding protein i mediates rapid non-canonical activation of ERK1/2 by all-trans retinoic acid
    • S.D. Persaud, Y.W. Lin, C.Y. Wu, H. Kagechika, and L.N. Wei Cellular retinoic acid binding protein I mediates rapid non-canonical activation of ERK1/2 by all-trans retinoic acid Cell. Signal. 25 2013 19 25
    • (2013) Cell. Signal. , vol.25 , pp. 19-25
    • Persaud, S.D.1    Lin, Y.W.2    Wu, C.Y.3    Kagechika, H.4    Wei, L.N.5
  • 44
    • 77950358156 scopus 로고    scopus 로고
    • Retinoic acid orchestrates fibroblast growth factor signalling to drive embryonic stem cell differentiation
    • M.P. Stavridis, B.J. Collins, and K.G. Storey Retinoic acid orchestrates fibroblast growth factor signalling to drive embryonic stem cell differentiation Development 137 2010 881 890
    • (2010) Development , vol.137 , pp. 881-890
    • Stavridis, M.P.1    Collins, B.J.2    Storey, K.G.3
  • 45
    • 84863797067 scopus 로고    scopus 로고
    • MSK1 and nuclear receptor signaling
    • S. Arthur, L. Vermeulen, Landes Biosciences (Austin
    • A. Piskunov, and C. Rochette-Egly MSK1 and nuclear receptor signaling S. Arthur, L. Vermeulen, MSKs Landes Biosciences 2011 (Austin)
    • (2011) MSKs
    • Piskunov, A.1    Rochette-Egly, C.2
  • 46
    • 77956919550 scopus 로고    scopus 로고
    • Polycomb group protein displacement and gene activation through MSK-dependent H3K27me3S28 phosphorylation
    • S.S. Gehani, S. Agrawal-Singh, N. Dietrich, N.S. Christophersen, K. Helin, and K. Hansen Polycomb group protein displacement and gene activation through MSK-dependent H3K27me3S28 phosphorylation Mol. Cell 39 2010 886 900
    • (2010) Mol. Cell , vol.39 , pp. 886-900
    • Gehani, S.S.1    Agrawal-Singh, S.2    Dietrich, N.3    Christophersen, N.S.4    Helin, K.5    Hansen, K.6
  • 49
    • 34547483059 scopus 로고    scopus 로고
    • Response of SMRT (silencing mediator of retinoic acid and thyroid hormone receptor) and N-CoR (nuclear receptor corepressor) corepressors to mitogen-activated protein kinase kinase kinase cascades is determined by alternative mRNA splicing
    • B.A. Jonas, N. Varlakhanova, F. Hayakawa, M. Goodson, and M.L. Privalsky Response of SMRT (silencing mediator of retinoic acid and thyroid hormone receptor) and N-CoR (nuclear receptor corepressor) corepressors to mitogen-activated protein kinase kinase kinase cascades is determined by alternative mRNA splicing Mol. Endocrinol. 21 2007 1924 1939
    • (2007) Mol. Endocrinol. , vol.21 , pp. 1924-1939
    • Jonas, B.A.1    Varlakhanova, N.2    Hayakawa, F.3    Goodson, M.4    Privalsky, M.L.5
  • 50
    • 21744435965 scopus 로고    scopus 로고
    • Controlling nuclear receptors: The circular logic of cofactor cycles
    • V. Perissi, and M.G. Rosenfeld Controlling nuclear receptors: the circular logic of cofactor cycles Nat. Rev. Mol. Cell Biol. 6 2005 542 554
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 542-554
    • Perissi, V.1    Rosenfeld, M.G.2
  • 51
    • 78650521041 scopus 로고    scopus 로고
    • Regulation of SMRT corepressor dimerization and composition by MAP kinase phosphorylation
    • N. Varlakhanova, J.B. Hahm, and M.L. Privalsky Regulation of SMRT corepressor dimerization and composition by MAP kinase phosphorylation Mol. Cell. Endocrinol. 332 2011 180 188
    • (2011) Mol. Cell. Endocrinol. , vol.332 , pp. 180-188
    • Varlakhanova, N.1    Hahm, J.B.2    Privalsky, M.L.3
  • 52
    • 12844281209 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase contributes to aberrant retinoid signaling in lung cancer cells by phosphorylating and inducing proteasomal degradation of retinoic acid receptor alpha
    • H. Srinivas, D.M. Juroske, S. Kalyankrishna, D.D. Cody, R.E. Price, X.C. Xu, R. Narayanan, N.L. Weigel, and J.M. Kurie c-Jun N-terminal kinase contributes to aberrant retinoid signaling in lung cancer cells by phosphorylating and inducing proteasomal degradation of retinoic acid receptor alpha Mol. Cell. Biol. 25 2005 1054 1069
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 1054-1069
    • Srinivas, H.1    Juroske, D.M.2    Kalyankrishna, S.3    Cody, D.D.4    Price, R.E.5    Xu, X.C.6    Narayanan, R.7    Weigel, N.L.8    Kurie, J.M.9
  • 53
    • 0037399647 scopus 로고    scopus 로고
    • Nuclear receptors: Integration of multiple signalling pathways through phosphorylation
    • C. Rochette-Egly Nuclear receptors: integration of multiple signalling pathways through phosphorylation Cell. Signal. 15 2003 355 366
    • (2003) Cell. Signal. , vol.15 , pp. 355-366
    • Rochette-Egly, C.1
  • 55
    • 77952296807 scopus 로고    scopus 로고
    • Loss of CAK phosphorylation of RAR{alpha} mediates transcriptional control of retinoid-induced cancer cell differentiation
    • A. Wang, I.N. Alimova, P. Luo, A. Jong, T.J. Triche, and L. Wu Loss of CAK phosphorylation of RAR{alpha} mediates transcriptional control of retinoid-induced cancer cell differentiation FASEB J. 24 2010 833 843
    • (2010) FASEB J. , vol.24 , pp. 833-843
    • Wang, A.1    Alimova, I.N.2    Luo, P.3    Jong, A.4    Triche, T.J.5    Wu, L.6
  • 56
    • 28044440089 scopus 로고    scopus 로고
    • Cyclin H binding to the RARalpha activation function (AF)-2 domain directs phosphorylation of the AF-1 domain by cyclin-dependent kinase 7
    • G. Bour, E. Gaillard, N. Bruck, S. Lalevee, J.L. Plassat, D. Busso, J.P. Samama, and C. Rochette-Egly Cyclin H binding to the RARalpha activation function (AF)-2 domain directs phosphorylation of the AF-1 domain by cyclin-dependent kinase 7 Proc. Natl. Acad. Sci. U. S. A. 102 2005 16608 16613
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 16608-16613
    • Bour, G.1    Gaillard, E.2    Bruck, N.3    Lalevee, S.4    Plassat, J.L.5    Busso, D.6    Samama, J.P.7    Rochette-Egly, C.8
  • 57
    • 84876907320 scopus 로고    scopus 로고
    • Phosphorylation of the retinoic acid receptor alpha induces a mechanical allosteric regulation and changes in internal dynamics
    • Y. Chebaro, I. Amal, N. Rochel, C. Rochette-Egly, R. Stote, and A. Dejaegere Phosphorylation of the retinoic acid receptor alpha induces a mechanical allosteric regulation and changes in internal dynamics PLoS Comput. Biol. 9 2013 e1003012
    • (2013) PLoS Comput. Biol. , vol.9 , pp. 1003012
    • Chebaro, Y.1    Amal, I.2    Rochel, N.3    Rochette-Egly, C.4    Stote, R.5    Dejaegere, A.6
  • 58
    • 33745465398 scopus 로고    scopus 로고
    • Phosphorylation by PKA potentiates retinoic acid receptor alpha activity by means of increasing interaction with and phosphorylation by cyclin H/cdk7
    • E. Gaillard, N. Bruck, Y. Brelivet, G. Bour, S. Lalevee, A. Bauer, O. Poch, D. Moras, and C. Rochette-Egly Phosphorylation by PKA potentiates retinoic acid receptor alpha activity by means of increasing interaction with and phosphorylation by cyclin H/cdk7 Proc. Natl. Acad. Sci. U. S. A. 103 2006 9548 9553
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 9548-9553
    • Gaillard, E.1    Bruck, N.2    Brelivet, Y.3    Bour, G.4    Lalevee, S.5    Bauer, A.6    Poch, O.7    Moras, D.8    Rochette-Egly, C.9
  • 60
    • 0037023499 scopus 로고    scopus 로고
    • XPD mutations prevent TFIIH-dependent transactivation by nuclear receptors and phosphorylation of RARalpha
    • A. Keriel, A. Stary, A. Sarasin, C. Rochette-Egly, and J.M. Egly XPD mutations prevent TFIIH-dependent transactivation by nuclear receptors and phosphorylation of RARalpha Cell 109 2002 125 135
    • (2002) Cell , vol.109 , pp. 125-135
    • Keriel, A.1    Stary, A.2    Sarasin, A.3    Rochette-Egly, C.4    Egly, J.M.5
  • 61
    • 68549094657 scopus 로고    scopus 로고
    • Stem cells, signals and vertebrate body axis extension
    • V. Wilson, I. Olivera-Martinez, and K.G. Storey Stem cells, signals and vertebrate body axis extension Development 136 2009 1591 1604
    • (2009) Development , vol.136 , pp. 1591-1604
    • Wilson, V.1    Olivera-Martinez, I.2    Storey, K.G.3
  • 62
    • 34250192881 scopus 로고    scopus 로고
    • Generation of a defined and uniform population of CNS progenitors and neurons from mouse embryonic stem cells
    • M. Bibel, J. Richter, E. Lacroix, and Y.A. Barde Generation of a defined and uniform population of CNS progenitors and neurons from mouse embryonic stem cells Nat. Protoc. 2 2007 1034 1043
    • (2007) Nat. Protoc. , vol.2 , pp. 1034-1043
    • Bibel, M.1    Richter, J.2    Lacroix, E.3    Barde, Y.A.4
  • 65
    • 77954174222 scopus 로고    scopus 로고
    • Activation of retinoic acid receptor signaling coordinates lineage commitment of spontaneously differentiating mouse embryonic stem cells in embryoid bodies
    • Z. Simandi, B.L. Balint, S. Poliska, R. Ruhl, and L. Nagy Activation of retinoic acid receptor signaling coordinates lineage commitment of spontaneously differentiating mouse embryonic stem cells in embryoid bodies FEBS Lett. 584 2010 3123 3130
    • (2010) FEBS Lett. , vol.584 , pp. 3123-3130
    • Simandi, Z.1    Balint, B.L.2    Poliska, S.3    Ruhl, R.4    Nagy, L.5
  • 66
    • 0033950079 scopus 로고    scopus 로고
    • The importance of being proline: The interaction of proline-rich motifs in signaling proteins with their cognate domains
    • B.K. Kay, M.P. Williamson, and M. Sudol The importance of being proline: the interaction of proline-rich motifs in signaling proteins with their cognate domains FASEB J. 14 2000 231 241
    • (2000) FASEB J. , vol.14 , pp. 231-241
    • Kay, B.K.1    Williamson, M.P.2    Sudol, M.3
  • 67
    • 0037138411 scopus 로고    scopus 로고
    • WW and SH3 domains, two different scaffolds to recognize proline-rich ligands
    • M.J. Macias, S. Wiesner, and M. Sudol WW and SH3 domains, two different scaffolds to recognize proline-rich ligands FEBS Lett. 513 2002 30 37
    • (2002) FEBS Lett. , vol.513 , pp. 30-37
    • Macias, M.J.1    Wiesner, S.2    Sudol, M.3
  • 68
    • 20444453254 scopus 로고    scopus 로고
    • Vinexin beta interacts with the non-phosphorylated AF-1 domain of retinoid receptor gamma (RARg) and represses RARg-mediated transcription
    • G. Bour, J.L. Plassat, A. Bauer, S. Lalevee, and C. Rochette-Egly Vinexin beta interacts with the non-phosphorylated AF-1 domain of retinoid receptor gamma (RARg) and represses RARg-mediated transcription J. Biol. Chem. 280 2005 17027 17037
    • (2005) J. Biol. Chem. , vol.280 , pp. 17027-17037
    • Bour, G.1    Plassat, J.L.2    Bauer, A.3    Lalevee, S.4    Rochette-Egly, C.5
  • 69
    • 82655171926 scopus 로고    scopus 로고
    • Structural analysis of nuclear receptors: From isolated domains to integral proteins
    • Y. Brelivet, N. Rochel, and D. Moras Structural analysis of nuclear receptors: from isolated domains to integral proteins Mol. Cell. Endocrinol. 348 2012 466 473
    • (2012) Mol. Cell. Endocrinol. , vol.348 , pp. 466-473
    • Brelivet, Y.1    Rochel, N.2    Moras, D.3
  • 71
    • 0029741380 scopus 로고    scopus 로고
    • Restricted expression of a novel retinoic acid responsive gene during limb bud dorsoventral patterning and endochondral ossification
    • C. Chazaud, P. Bouillet, M. Oulad-Abdelghani, and P. Dolle Restricted expression of a novel retinoic acid responsive gene during limb bud dorsoventral patterning and endochondral ossification Dev. Genet. 19 1996 66 73
    • (1996) Dev. Genet. , vol.19 , pp. 66-73
    • Chazaud, C.1    Bouillet, P.2    Oulad-Abdelghani, M.3    Dolle, P.4
  • 73
    • 70349897766 scopus 로고    scopus 로고
    • The posteriorizing gene Gbx2 is a direct target of Wnt signalling and the earliest factor in neural crest induction
    • B. Li, S. Kuriyama, M. Moreno, and R. Mayor The posteriorizing gene Gbx2 is a direct target of Wnt signalling and the earliest factor in neural crest induction Development 136 2009 3267 3278
    • (2009) Development , vol.136 , pp. 3267-3278
    • Li, B.1    Kuriyama, S.2    Moreno, M.3    Mayor, R.4
  • 74
    • 37349052866 scopus 로고    scopus 로고
    • Inhibition of Activin/Nodal signaling promotes specification of human embryonic stem cells into neuroectoderm
    • J.R. Smith, L. Vallier, G. Lupo, M. Alexander, W.A. Harris, and R.A. Pedersen Inhibition of Activin/Nodal signaling promotes specification of human embryonic stem cells into neuroectoderm Dev. Biol. 313 2008 107 117
    • (2008) Dev. Biol. , vol.313 , pp. 107-117
    • Smith, J.R.1    Vallier, L.2    Lupo, G.3    Alexander, M.4    Harris, W.A.5    Pedersen, R.A.6
  • 75
    • 79951522779 scopus 로고    scopus 로고
    • Gbx2 and Fgf8 are sequentially required for formation of the midbrain-hindbrain compartment boundary
    • N.A. Sunmonu, K. Li, Q. Guo, and J.Y. Li Gbx2 and Fgf8 are sequentially required for formation of the midbrain-hindbrain compartment boundary Development 138 2011 725 734
    • (2011) Development , vol.138 , pp. 725-734
    • Sunmonu, N.A.1    Li, K.2    Guo, Q.3    Li, J.Y.4
  • 76
    • 38949111026 scopus 로고    scopus 로고
    • Gene expression profiling elucidates a specific role for RARgamma in the retinoic acid-induced differentiation of F9 teratocarcinoma stem cells
    • D. Su, and L.J. Gudas Gene expression profiling elucidates a specific role for RARgamma in the retinoic acid-induced differentiation of F9 teratocarcinoma stem cells Biochem. Pharmacol. 75 2008 1129 1160
    • (2008) Biochem. Pharmacol. , vol.75 , pp. 1129-1160
    • Su, D.1    Gudas, L.J.2
  • 77
    • 67549104319 scopus 로고    scopus 로고
    • Genomic antagonism between retinoic acid and estrogen signaling in breast cancer
    • S. Hua, R. Kittler, and K.P. White Genomic antagonism between retinoic acid and estrogen signaling in breast cancer Cell 137 2009 1259 1271
    • (2009) Cell , vol.137 , pp. 1259-1271
    • Hua, S.1    Kittler, R.2    White, K.P.3
  • 79
    • 84879264708 scopus 로고    scopus 로고
    • ZFN, TALEN, and CRISPR/Cas-based methods for genome engineering
    • T. Gaj, C.A. Gersbach, and C.F. Barbas III ZFN, TALEN, and CRISPR/Cas-based methods for genome engineering Trends Biotechnol. 31 2013 397 405
    • (2013) Trends Biotechnol. , vol.31 , pp. 397-405
    • Gaj, T.1    Gersbach, C.A.2    Barbas, C.F.3


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