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Volumn 61, Issue 6, 2009, Pages 670-678

p38 mitogen-activated protein kinase-dependent regulation of SRC-3 and involvement in retinoic acid receptor α signaling in embryonic cortical neurons

Author keywords

All trans retinoic acid; Neuron; p38 mitogen activated protein kinase; Retinoic acid receptor; SRC 3

Indexed keywords

4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; MITOGEN ACTIVATED PROTEIN KINASE P38; RETINOIC ACID RECEPTOR ALPHA; STEROID RECEPTOR COACTIVATOR 3; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR HOXD3; UNCLASSIFIED DRUG; DNA BINDING PROTEIN; HISTONE ACETYLTRANSFERASE; HOXD3 PROTEIN, MOUSE; NUCLEAR RECEPTOR COACTIVATOR 3; RETINOIC ACID; RETINOIC ACID RECEPTOR; TRANSACTIVATOR PROTEIN;

EID: 69449085554     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.212     Document Type: Article
Times cited : (14)

References (32)
  • 1
    • 0036832158 scopus 로고    scopus 로고
    • Retinoid signalling in the development of the central nervous system
    • Maden, M. (2002) Retinoid signalling in the development of the central nervous system. Nat. Rev. Neurosci. 3, 843-853.
    • (2002) Nat. Rev. Neurosci. , vol.3 , pp. 843-853
    • Maden, M.1
  • 2
    • 0030850655 scopus 로고    scopus 로고
    • A behavioral and neuroanatomical investigation of the lethality caused by gestational day 11-13 retinoic acid exposure
    • Holson, R. R., Gazzara, R. A., Ferguson, S. A., and Adams, J. (1997a) A behavioral and neuroanatomical investigation of the lethality caused by gestational day 11-13 retinoic acid exposure. Neurotoxicol. Teratol. 19, 347-353.
    • (1997) Neurotoxicol. Teratol. , vol.19 , pp. 347-353
    • Holson, R.R.1    Gazzara, R.A.2    Ferguson, S.A.3    Adams, J.4
  • 3
    • 0030827060 scopus 로고    scopus 로고
    • Gestational retinoic acid exposure: A sensitive period for effects on neonatal mortality and cerebellar development
    • Holson, R. R., Gazzara, R. A., Ferguson, S. A., Ali, S. F., Laborde, J. B., and Adams, J. (1997b) Gestational retinoic acid exposure: a sensitive period for effects on neonatal mortality and cerebellar development. Neurotoxicol. Teratol. 19, 335-346.
    • (1997) Neurotoxicol. Teratol. , vol.19 , pp. 335-346
    • Holson, R.R.1    Gazzara, R.A.2    Ferguson, S.A.3    Ali, S.F.4    Laborde, J.B.5    Adams, J.6
  • 6
    • 34447326960 scopus 로고    scopus 로고
    • Retinoic acid regulation of the somitogenesis clock
    • Duester, G. (2007) Retinoic acid regulation of the somitogenesis clock. Birth Defects Res. C Embryo Today 81, 84-92.
    • (2007) Birth Defects Res. C Embryo Today , vol.81 , pp. 84-92
    • Duester, G.1
  • 7
    • 34648816863 scopus 로고    scopus 로고
    • Retinoic acid in the development, regeneration and maintenance of the nervous system
    • Maden, M. (2007) Retinoic acid in the development, regeneration and maintenance of the nervous system. Nat. Rev. Neurosci. 8, 755-765.
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 755-765
    • Maden, M.1
  • 8
    • 1542710344 scopus 로고    scopus 로고
    • Nuclear retinoid receptors and the transcription of retinoid-target genes
    • DOI 10.1016/j.gene.2003.12.005, PII S0378111903011296
    • Bastien, J. and Rochette-Egly, C. (2004) Nuclear retinoid receptors and the transcription of retinoid-target genes. Gene 328, 1-16. (Pubitemid 38352876)
    • (2004) Gene , vol.328 , Issue.1-2 , pp. 1-16
    • Bastien, J.1    Rochette-Egly, C.2
  • 9
    • 25444455856 scopus 로고    scopus 로고
    • Dynamic combinatorial networks in nuclear receptor-mediated transcription
    • Rochette-Egly, C. (2005) Dynamic combinatorial networks in nuclear receptor-mediated transcription. J. Biol. Chem. 280, 32565-32568.
    • (2005) J. Biol. Chem. , vol.280 , pp. 32565-32568
    • Rochette-Egly, C.1
  • 10
    • 0029794132 scopus 로고    scopus 로고
    • A decade of molecular biology of retinoic acid receptors
    • Chambon, P. (1996) A decade of molecular biology of retinoic acid receptors. FASEB J. 10, 940-954. (Pubitemid 26285969)
    • (1996) FASEB Journal , vol.10 , Issue.9 , pp. 940-954
    • Chambon, P.1
  • 11
    • 0035957953 scopus 로고    scopus 로고
    • CREB-binding protein and p300 in transcriptional regulation
    • Vo, N. and Goodman, R. H. (2001) CREB-binding protein and p300 in transcriptional regulation. J. Biol. Chem. 276, 13505-13508.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13505-13508
    • Vo, N.1    Goodman, R.H.2
  • 12
    • 18844373937 scopus 로고    scopus 로고
    • Transcriptional regulation by steroid receptor coactivator phosphorylation
    • Wu, R. C., Smith, C. L., and O'Malley, B. W. (2005) Transcriptional regulation by steroid receptor coactivator phosphorylation. Endocr. Rev. 26, 393-399.
    • (2005) Endocr. Rev. , vol.26 , pp. 393-399
    • Wu, R.C.1    Smith, C.L.2    O'Malley, B.W.3
  • 13
    • 33644529089 scopus 로고    scopus 로고
    • P38MAPK-dependent phosphorylation and degradation of SRC-3/AIB1 and RARalpha-mediated transcription
    • DOI 10.1038/sj.emboj.7600981, PII 7600981
    • Gianni, M., Parrella, E., Raska, I. Jr., Gaillard, E., Nigro, E. A., Gaudon, C., Garattini, E., and Rochette-Egly, C. (2006) P38MAPK-dependent phosphorylation and degradation of SRC-3/AIB1 and RARalpha-mediated transcription. EMBO J. 25, 739-751. (Pubitemid 43292436)
    • (2006) EMBO Journal , vol.25 , Issue.4 , pp. 739-751
    • Gianni, M.1    Parrella, E.2    Raska Jr., I.3    Gaillard, E.4    Nigro, E.A.5    Gaudon, C.6    Garattini, E.7    Rochette-Egly, C.8
  • 14
    • 0001392322 scopus 로고    scopus 로고
    • AIB1 is a conduit for kinase-mediated growth factor signaling to the estrogen receptor
    • Font de Mora, J. and Brown, M. (2000) AIB1 is a conduit for kinase-mediated growth factor signaling to the estrogen receptor. Mol. Cell. Biol. 20, 5041-5047.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 5041-5047
    • Font De Mora, J.1    Brown, M.2
  • 15
    • 4644252581 scopus 로고    scopus 로고
    • Selective phosphorylations of the SRC-3/AIB1 coactivator integrate genomic reponses to multiple cellular signaling pathways
    • Wu, R. C., Qin, J., Yi, P., Wong, J., Tsai, S. Y., Tsai, M. J., and O'Malley, B. W. (2004) Selective phosphorylations of the SRC-3/AIB1 coactivator integrate genomic reponses to multiple cellular signaling pathways. Mol. Cell. 15, 937-949.
    • (2004) Mol. Cell. , vol.15 , pp. 937-949
    • Wu, R.C.1    Qin, J.2    Yi, P.3    Wong, J.4    Tsai, S.Y.5    Tsai, M.J.6    O'Malley, B.W.7
  • 16
    • 0036242554 scopus 로고    scopus 로고
    • Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/TRAM-1) coactivator activity by I kappa B kinase
    • Wu, R. C., Qin, J., Hashimoto, Y., Wong, J., Xu, J., Tsai, S. Y., Tsai, M. J., and O'Malley, B. W. (2002) Regulation of SRC-3 (pCIP/ACTR/AIB-1/RAC-3/ TRAM-1) coactivator activity by I kappa B kinase. Mol. Cell. Biol. 22, 3549-3561.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3549-3561
    • Wu, R.C.1    Qin, J.2    Hashimoto, Y.3    Wong, J.4    Xu, J.5    Tsai, S.Y.6    Tsai, M.J.7    O'Malley, B.W.8
  • 17
    • 34250001084 scopus 로고    scopus 로고
    • SRC-3 Coactivator Functional Lifetime Is Regulated by a Phospho-Dependent Ubiquitin Time Clock
    • DOI 10.1016/j.cell.2007.04.039, PII S0092867407005855
    • Wu, R. C., Feng, Q., Lonard, D. M, and O'Malley, B. W. (2007) SRC-3 coactivator functional lifetime is regulated by a phospho-dependent ubiquitin time clock. Cell 129, 1125-1140. (Pubitemid 46891039)
    • (2007) Cell , vol.129 , Issue.6 , pp. 1125-1140
    • Wu, R.-C.1    Feng, Q.2    Lonard, D.M.3    O'Malley, B.W.4
  • 18
    • 39749194927 scopus 로고    scopus 로고
    • Atypical protein kinase C regulates dual pathways for degradation of the oncogenic coactivator SRC-3/AIB1
    • Yi, P., Feng, Q., Amazit, L., Lonard, D. M., Tsai, S. Y., Tsai, M. J., and O'Malley, B. W. (2008) Atypical protein kinase C regulates dual pathways for degradation of the oncogenic coactivator SRC-3/AIB1. Mol. Cell. 29, 465-476.
    • (2008) Mol. Cell. , vol.29 , pp. 465-476
    • Yi, P.1    Feng, Q.2    Amazit, L.3    Lonard, D.M.4    Tsai, S.Y.5    Tsai, M.J.6    O'Malley, B.W.7
  • 19
    • 0141925793 scopus 로고    scopus 로고
    • The coactivator p/CIP/SRC-3 facilitates retinoic acid receptor signaling via recruitment of GCN5
    • Brown, K., Chen, Y., Underhill, T. M., Mymryk, J. S., and Torchia, J. (2003) The coactivator p/CIP/SRC-3 facilitates retinoic acid receptor signaling via recruitment of GCN5. J. Biol. Chem. 278, 39402-39412.
    • (2003) J. Biol. Chem. , vol.278 , pp. 39402-39412
    • Brown, K.1    Chen, Y.2    Underhill, T.M.3    Mymryk, J.S.4    Torchia, J.5
  • 21
  • 22
    • 0035881448 scopus 로고    scopus 로고
    • Active repression of RAR signaling is required for head formation
    • DOI 10.1101/gad.908801
    • Koide, T., Downes, M., Chandraratna, R. A., Blumberg, B., and Umesono, K. (2001) Active repression of RAR signaling is required for head formation. Genes Dev. 15, 2111-2121. (Pubitemid 32762054)
    • (2001) Genes and Development , vol.15 , Issue.16 , pp. 2111-2121
    • Koide, T.1    Downes, M.2    Chandraratna, R.A.S.3    Blumberg, B.4    Umesono, K.5
  • 23
    • 0036862406 scopus 로고    scopus 로고
    • Initiating Hox gene expression: In the early chick neural tube differential sensitivity to FGF and RA signaling subdivides the HoxB genes in two distinct groups
    • Bel-Vialar, S., Itasaki, N., and Krumlauf, R. (2002) Initiating Hox gene expression: in the early chick neural tube differential sensitivity to FGF and RA signaling subdivides the HoxB genes in two distinct groups. Development 129, 5103-5115. (Pubitemid 35460675)
    • (2002) Development , vol.129 , Issue.22 , pp. 5103-5115
    • Bel-Vialar, S.1    Itasaki, N.2    Krumlauf, R.3
  • 25
    • 36348956805 scopus 로고    scopus 로고
    • Brevetoxin-induced phosphorylation of Pyk2 and Src in murine neocortical neurons involves distinct signaling pathways
    • DOI 10.1016/j.brainres.2007.09.065, PII S0006899307022822
    • Cao, Z., George, J., Baden, D. G., and Murray, T. F. (2007) Brevetoxin-induced phosphorylation of Pyk2 and Src in murine neocortical neurons involves distinct signaling pathways. Brain Res. 1184, 17-27. (Pubitemid 350160585)
    • (2007) Brain Research , vol.1184 , Issue.1 , pp. 17-27
    • Cao, Z.1    George, J.2    Baden, D.G.3    Murray, T.F.4
  • 27
    • 24644497683 scopus 로고    scopus 로고
    • Rapid estrogen-induced phosphorylation of the SRC-3 coactivator occurs in an extranuclear complex containing estrogen receptor
    • Zheng, F. F., Wu, R. C., Smith, C. L., and O'Malley, B. W. (2005) Rapid estrogen-induced phosphorylation of the SRC-3 coactivator occurs in an extranuclear complex containing estrogen receptor. Mol. Cell. Biol. 25, 8273-8284.
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 8273-8284
    • Zheng, F.F.1    Wu, R.C.2    Smith, C.L.3    O'Malley, B.W.4
  • 28
    • 0035937734 scopus 로고    scopus 로고
    • Control of retinoic acid receptor heterodimerization by ligand-induced structural transitions. A novel mechanism of action for retinoid antagonists
    • Depoix, C., Delmotte, M. H., Formstecher, P., and Lefebvre, P. (2001) Control of retinoic acid receptor heterodimerization by ligand-induced structural transitions. A novel mechanism of action for retinoid antagonists. J. Biol. Chem. 276, 9452-9459.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9452-9459
    • Depoix, C.1    Delmotte, M.H.2    Formstecher, P.3    Lefebvre, P.4
  • 29
    • 0034161266 scopus 로고    scopus 로고
    • Structure of the RXR-RAR DNA-binding complex on the retinoic acid response element DR1
    • Rastinejad, F., Wagner, T., Zhao, Q., and Khorasanizadeh, S. (2000) Structure of the RXR-RAR DNA-binding complex on the retinoic acid response element DR1. EMBO J. 19, 1045-1054. (Pubitemid 30119829)
    • (2000) EMBO Journal , vol.19 , Issue.5 , pp. 1045-1054
    • Rastinejad, F.1    Wagner, T.2    Zhao, Q.3    Khorasanizadeh, S.4
  • 30
    • 7444247424 scopus 로고    scopus 로고
    • Retinoic acid induces neuroblastoma cell death by inhibiting proteasomal degradation of retinoic acid receptor alpha
    • DOI 10.1158/0008-5472.CAN-04-1178
    • Nagai, J., Yazawa, T., Okudela, K., Kigasawa, H., Kitamura, H., and Osaka, H. (2004) Retinoic acid induces neuroblastoma cell death by inhibiting proteasomal degradation of retinoic acid receptor alpha. Cancer Res. 64, 7910-7917. (Pubitemid 39446924)
    • (2004) Cancer Research , vol.64 , Issue.21 , pp. 7910-7917
    • Nagai, J.-I.1    Yazawa, T.2    Okudela, K.3    Kigasawa, H.4    Kitamura, H.5    Osaka, H.6
  • 31
    • 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
    • Srinivas, H., Juroske, D. M., Kalyankrishna, S., Cody, D. D., Price, R. E., Xu, X. C., Narayanan, R., Weigel, N. L., and Kurie, J. M. (2005) 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, 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
  • 32
    • 0033592948 scopus 로고    scopus 로고
    • Retinoic acid induces proteasome-dependent degradation of retinoic acid receptor alpha (RARalpha) and oncogenic RARalpha fusion proteins
    • Zhu, J., Gianni, M., Kopf, E., Honore, N., Chelbi-Alix, M., Koken, M., Quignon, F., Rochette-Egly, C., and de The, H. (1999) Retinoic acid induces proteasome-dependent degradation of retinoic acid receptor alpha (RARalpha) and oncogenic RARalpha fusion proteins. Proc. Natl. Acad. Sci. USA 96, 14807-14812.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 14807-14812
    • Zhu, J.1    Gianni, M.2    Kopf, E.3    Honore, N.4    Chelbi-Alix, M.5    Koken, M.6    Quignon, F.7    Rochette-Egly, C.8    De The, H.9


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