메뉴 건너뛰기




Volumn 24, Issue 2, 2006, Pages 233-243

Two Functional Modes of a Nuclear Receptor-Recruited Arginine Methyltransferase in Transcriptional Activation

Author keywords

DNA

Indexed keywords

ACYLTRANSFERASE; ARGININE TRANSFER RNA LIGASE;

EID: 33749664150     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2006.09.020     Document Type: Article
Times cited : (88)

References (41)
  • 1
    • 0842282837 scopus 로고    scopus 로고
    • Reconstitution and transcriptional analysis of chromatin in vitro
    • An W., and Roeder R.G. Reconstitution and transcriptional analysis of chromatin in vitro. Methods Enzymol. 377 (2004) 460-474
    • (2004) Methods Enzymol. , vol.377 , pp. 460-474
    • An, W.1    Roeder, R.G.2
  • 2
    • 2942612843 scopus 로고    scopus 로고
    • Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53
    • An W., Kim J., and Roeder R.G. Ordered cooperative functions of PRMT1, p300, and CARM1 in transcriptional activation by p53. Cell 117 (2004) 735-748
    • (2004) Cell , vol.117 , pp. 735-748
    • An, W.1    Kim, J.2    Roeder, R.G.3
  • 3
    • 20844450998 scopus 로고    scopus 로고
    • Arginine methylation: an emerging regulator of protein function
    • Bedford M.T., and Richard S. Arginine methylation: an emerging regulator of protein function. Mol. Cell 18 (2005) 263-272
    • (2005) Mol. Cell , vol.18 , pp. 263-272
    • Bedford, M.T.1    Richard, S.2
  • 4
    • 0028148776 scopus 로고
    • Disruption of the HNF-4 gene, expressed in visceral endoderm, leads to cell death in embryonic ectoderm and impaired gastrulation of mouse embryos
    • Chen W.S., Manova K., Weinstein D.C., Duncan S.A., Plump A.S., Prezioso V.R., Bachvarova R.F., and Darnell Jr. J.E. Disruption of the HNF-4 gene, expressed in visceral endoderm, leads to cell death in embryonic ectoderm and impaired gastrulation of mouse embryos. Genes Dev. 8 (1994) 2466-2477
    • (1994) Genes Dev. , vol.8 , pp. 2466-2477
    • Chen, W.S.1    Manova, K.2    Weinstein, D.C.3    Duncan, S.A.4    Plump, A.S.5    Prezioso, V.R.6    Bachvarova, R.F.7    Darnell Jr., J.E.8
  • 5
    • 0034731452 scopus 로고    scopus 로고
    • Synergistic, p160 coactivator-dependent enhancement of estrogen receptor function by CARM1 and p300
    • Chen D., Huang S.M., and Stallcup M.R. Synergistic, p160 coactivator-dependent enhancement of estrogen receptor function by CARM1 and p300. J. Biol. Chem. 275 (2000) 40810-40816
    • (2000) J. Biol. Chem. , vol.275 , pp. 40810-40816
    • Chen, D.1    Huang, S.M.2    Stallcup, M.R.3
  • 6
    • 25444520791 scopus 로고    scopus 로고
    • Effector proteins for methylated histones: an expanding family
    • Daniel J.A., Pray-Grant M.G., and Grant P.A. Effector proteins for methylated histones: an expanding family. Cell Cycle 4 (2005) 919-926
    • (2005) Cell Cycle , vol.4 , pp. 919-926
    • Daniel, J.A.1    Pray-Grant, M.G.2    Grant, P.A.3
  • 7
    • 0033605598 scopus 로고    scopus 로고
    • CREB-binding protein is a transcriptional coactivator for hepatocyte nuclear factor-4 and enhances apolipoprotein gene expression
    • Dell H., and Hadzopoulou-Cladaras M. CREB-binding protein is a transcriptional coactivator for hepatocyte nuclear factor-4 and enhances apolipoprotein gene expression. J. Biol. Chem. 274 (1999) 9013-9021
    • (1999) J. Biol. Chem. , vol.274 , pp. 9013-9021
    • Dell, H.1    Hadzopoulou-Cladaras, M.2
  • 8
    • 0037063997 scopus 로고    scopus 로고
    • Crystal structure of the HNF4 alpha ligand binding domain in complex with endogenous fatty acid ligand
    • Dhe-Paganon S., Duda K., Iwamoto M., Chi Y.I., and Shoelson S.E. Crystal structure of the HNF4 alpha ligand binding domain in complex with endogenous fatty acid ligand. J. Biol. Chem. 277 (2002) 37973-37976
    • (2002) J. Biol. Chem. , vol.277 , pp. 37973-37976
    • Dhe-Paganon, S.1    Duda, K.2    Iwamoto, M.3    Chi, Y.I.4    Shoelson, S.E.5
  • 10
    • 0035141324 scopus 로고    scopus 로고
    • Hepatocyte nuclear factor 4alpha (nuclear receptor 2A1) is essential for maintenance of hepatic gene expression and lipid homeostasis
    • Hayhurst G.P., Lee Y.H., Lambert G., Ward J.M., and Gonzalez F.J. Hepatocyte nuclear factor 4alpha (nuclear receptor 2A1) is essential for maintenance of hepatic gene expression and lipid homeostasis. Mol. Cell. Biol. 21 (2001) 1393-1403
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1393-1403
    • Hayhurst, G.P.1    Lee, Y.H.2    Lambert, G.3    Ward, J.M.4    Gonzalez, F.J.5
  • 11
    • 0032473950 scopus 로고    scopus 로고
    • Fatty acyl-CoA thioesters are ligands of hepatic nuclear factor-4alpha
    • Hertz R., Magenheim J., Berman I., and Bar-Tana J. Fatty acyl-CoA thioesters are ligands of hepatic nuclear factor-4alpha. Nature 392 (1998) 512-516
    • (1998) Nature , vol.392 , pp. 512-516
    • Hertz, R.1    Magenheim, J.2    Berman, I.3    Bar-Tana, J.4
  • 12
    • 23944435995 scopus 로고    scopus 로고
    • Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications
    • Huang S., Litt M., and Felsenfeld G. Methylation of histone H4 by arginine methyltransferase PRMT1 is essential in vivo for many subsequent histone modifications. Genes Dev. 19 (2005) 1885-1893
    • (2005) Genes Dev. , vol.19 , pp. 1885-1893
    • Huang, S.1    Litt, M.2    Felsenfeld, G.3
  • 13
    • 0035839136 scopus 로고    scopus 로고
    • Translating the histone code
    • Jenuwein T., and Allis C.D. Translating the histone code. Science 293 (2001) 1074-1080
    • (2001) Science , vol.293 , pp. 1074-1080
    • Jenuwein, T.1    Allis, C.D.2
  • 14
    • 0031127252 scopus 로고    scopus 로고
    • Serine/threonine phosphorylation of orphan receptor hepatocyte nuclear factor 4
    • Jiang G., Nepomuceno L., Yang Q., and Sladek F.M. Serine/threonine phosphorylation of orphan receptor hepatocyte nuclear factor 4. Arch. Biochem. Biophys. 340 (1997) 1-9
    • (1997) Arch. Biochem. Biophys. , vol.340 , pp. 1-9
    • Jiang, G.1    Nepomuceno, L.2    Yang, Q.3    Sladek, F.M.4
  • 15
    • 0035846953 scopus 로고    scopus 로고
    • Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities
    • Koh S.S., Chen D., Lee Y.H., and Stallcup M.R. Synergistic enhancement of nuclear receptor function by p160 coactivators and two coactivators with protein methyltransferase activities. J. Biol. Chem. 276 (2001) 1089-1098
    • (2001) J. Biol. Chem. , vol.276 , pp. 1089-1098
    • Koh, S.S.1    Chen, D.2    Lee, Y.H.3    Stallcup, M.R.4
  • 16
    • 0033635222 scopus 로고    scopus 로고
    • Activator-dependent transcription from chromatin in vitro involving targeted histone acetylation by p300
    • Kundu T.K., Palhan V.B., Wang Z., An W., Cole P.A., and Roeder R.G. Activator-dependent transcription from chromatin in vitro involving targeted histone acetylation by p300. Mol. Cell 6 (2000) 551-561
    • (2000) Mol. Cell , vol.6 , pp. 551-561
    • Kundu, T.K.1    Palhan, V.B.2    Wang, Z.3    An, W.4    Cole, P.A.5    Roeder, R.G.6
  • 17
    • 0036093624 scopus 로고    scopus 로고
    • Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities
    • Lee Y.H., Koh S.S., Zhang X., Cheng X., and Stallcup M.R. Synergy among nuclear receptor coactivators: selective requirement for protein methyltransferase and acetyltransferase activities. Mol. Cell. Biol. 22 (2002) 3621-3632
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 3621-3632
    • Lee, Y.H.1    Koh, S.S.2    Zhang, X.3    Cheng, X.4    Stallcup, M.R.5
  • 18
    • 0035940497 scopus 로고    scopus 로고
    • Sequential recruitment of steroid receptor coactivator-1 (SRC-1) and p300 enhances progesterone receptor-dependent initiation and reinitiation of transcription from chromatin
    • Liu Z., Wong J., Tsai S.Y., Tsai M.J., and O'Malley B.W. Sequential recruitment of steroid receptor coactivator-1 (SRC-1) and p300 enhances progesterone receptor-dependent initiation and reinitiation of transcription from chromatin. Proc. Natl. Acad. Sci. USA 98 (2001) 12426-12431
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 12426-12431
    • Liu, Z.1    Wong, J.2    Tsai, S.Y.3    Tsai, M.J.4    O'Malley, B.W.5
  • 19
    • 0842347706 scopus 로고    scopus 로고
    • Techniques used to study transcription on chromatin templates
    • Loyola A., He S., Oh S., McCafferty D.G., and Reinberg D. Techniques used to study transcription on chromatin templates. Methods Enzymol. 377 (2004) 474-499
    • (2004) Methods Enzymol. , vol.377 , pp. 474-499
    • Loyola, A.1    He, S.2    Oh, S.3    McCafferty, D.G.4    Reinberg, D.5
  • 20
    • 0242643039 scopus 로고    scopus 로고
    • Study of nuclear receptor-induced transcription complex assembly and histone modification by chromatin immunoprecipitation assays
    • Ma H., Shang Y., Lee D.Y., and Stallcup M.R. Study of nuclear receptor-induced transcription complex assembly and histone modification by chromatin immunoprecipitation assays. Methods Enzymol. 364 (2003) 284-296
    • (2003) Methods Enzymol. , vol.364 , pp. 284-296
    • Ma, H.1    Shang, Y.2    Lee, D.Y.3    Stallcup, M.R.4
  • 21
    • 0036019471 scopus 로고    scopus 로고
    • Polyamines modulate the interaction between nuclear receptors and vitamin D receptor-interacting protein 205
    • Maeda Y., Rachez C., Hawel III L., Byus C.V., Freedman L.P., and Sladek F.M. Polyamines modulate the interaction between nuclear receptors and vitamin D receptor-interacting protein 205. Mol. Endocrinol. 16 (2002) 1502-1510
    • (2002) Mol. Endocrinol. , vol.16 , pp. 1502-1510
    • Maeda, Y.1    Rachez, C.2    Hawel III, L.3    Byus, C.V.4    Freedman, L.P.5    Sladek, F.M.6
  • 22
    • 3242666367 scopus 로고    scopus 로고
    • Transcriptional regulation of the apolipoprotein AI gene
    • Malik S. Transcriptional regulation of the apolipoprotein AI gene. Front. Biosci. 8 (2003) d360-d368
    • (2003) Front. Biosci. , vol.8
    • Malik, S.1
  • 23
    • 0029865801 scopus 로고    scopus 로고
    • TFIIB-directed transcriptional activation by the orphan nuclear receptor hepatocyte nuclear factor 4
    • Malik S., and Karathanasis S.K. TFIIB-directed transcriptional activation by the orphan nuclear receptor hepatocyte nuclear factor 4. Mol. Cell. Biol. 16 (1996) 1824-1831
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1824-1831
    • Malik, S.1    Karathanasis, S.K.2
  • 24
    • 0242474613 scopus 로고    scopus 로고
    • Isolation and functional characterization of the TRAP/Mediator complex
    • Malik S., and Roeder R.G. Isolation and functional characterization of the TRAP/Mediator complex. Methods Enzymol. 364 (2003) 257-284
    • (2003) Methods Enzymol. , vol.364 , pp. 257-284
    • Malik, S.1    Roeder, R.G.2
  • 25
    • 0036318299 scopus 로고    scopus 로고
    • TRAP/SMCC/Mediator-dependent transcriptional activation from DNA and chromatin templates by orphan nuclear receptor hepatocyte nuclear factor 4
    • Malik S., Wallberg A.E., Kang Y.K., and Roeder R.G. TRAP/SMCC/Mediator-dependent transcriptional activation from DNA and chromatin templates by orphan nuclear receptor hepatocyte nuclear factor 4. Mol. Cell. Biol. 22 (2002) 5626-5637
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 5626-5637
    • Malik, S.1    Wallberg, A.E.2    Kang, Y.K.3    Roeder, R.G.4
  • 26
    • 25444455856 scopus 로고    scopus 로고
    • Dynamic combinatorial networks in nuclear receptor-mediated transcription
    • Rochette-Egly C. Dynamic combinatorial networks in nuclear receptor-mediated transcription. J. Biol. Chem. 280 (2005) 32565-32568
    • (2005) J. Biol. Chem. , vol.280 , pp. 32565-32568
    • Rochette-Egly, C.1
  • 27
    • 14544280757 scopus 로고    scopus 로고
    • Transcriptional regulation and the role of diverse coactivators in animal cells
    • Roeder R.G. Transcriptional regulation and the role of diverse coactivators in animal cells. FEBS Lett. 579 (2005) 909-915
    • (2005) FEBS Lett. , vol.579 , pp. 909-915
    • Roeder, R.G.1
  • 28
    • 0027662208 scopus 로고
    • Orphan receptor HNF-4 and liver-specific gene expression
    • Sladek F.M. Orphan receptor HNF-4 and liver-specific gene expression. Receptor 3 (1993) 223-232
    • (1993) Receptor , vol.3 , pp. 223-232
    • Sladek, F.M.1
  • 29
    • 0025690311 scopus 로고
    • Liver-enriched transcription factor HNF-4 is a novel member of the steroid hormone receptor superfamily
    • Sladek F.M., Zhong W.M., Lai E., and Darnell Jr. J.E. Liver-enriched transcription factor HNF-4 is a novel member of the steroid hormone receptor superfamily. Genes Dev. 4 (1990) 2353-2365
    • (1990) Genes Dev. , vol.4 , pp. 2353-2365
    • Sladek, F.M.1    Zhong, W.M.2    Lai, E.3    Darnell Jr., J.E.4
  • 30
    • 0037040550 scopus 로고    scopus 로고
    • Coordination of PIC assembly and chromatin remodeling during differentiation-induced gene activation
    • Soutoglou E., and Talianidis I. Coordination of PIC assembly and chromatin remodeling during differentiation-induced gene activation. Science 295 (2002) 1901-1904
    • (2002) Science , vol.295 , pp. 1901-1904
    • Soutoglou, E.1    Talianidis, I.2
  • 31
    • 0033636892 scopus 로고    scopus 로고
    • Acetylation regulates transcription factor activity at multiple levels
    • Soutoglou E., Katrakili N., and Talianidis I. Acetylation regulates transcription factor activity at multiple levels. Mol. Cell 5 (2000) 745-751
    • (2000) Mol. Cell , vol.5 , pp. 745-751
    • Soutoglou, E.1    Katrakili, N.2    Talianidis, I.3
  • 32
    • 0035962649 scopus 로고    scopus 로고
    • Role of protein methylation in chromatin remodeling and transcriptional regulation
    • Stallcup M.R. Role of protein methylation in chromatin remodeling and transcriptional regulation. Oncogene 20 (2001) 3014-3020
    • (2001) Oncogene , vol.20 , pp. 3014-3020
    • Stallcup, M.R.1
  • 34
    • 25444490098 scopus 로고    scopus 로고
    • An in vitro assay to study the recruitment and substrate specificity of chromatin modifying enzymes
    • Vermeulen M., and Stunnenberg H.G. An in vitro assay to study the recruitment and substrate specificity of chromatin modifying enzymes. Biol. Proced. Online 6 (2004) 157-162
    • (2004) Biol. Proced. Online , vol.6 , pp. 157-162
    • Vermeulen, M.1    Stunnenberg, H.G.2
  • 35
    • 0030877342 scopus 로고    scopus 로고
    • Protein kinase A-dependent phosphorylation modulates DNA-binding activity of hepatocyte nuclear factor 4
    • Viollet B., Kahn A., and Raymondjean M. Protein kinase A-dependent phosphorylation modulates DNA-binding activity of hepatocyte nuclear factor 4. Mol. Cell. Biol. 17 (1997) 4208-4219
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4208-4219
    • Viollet, B.1    Kahn, A.2    Raymondjean, M.3
  • 36
    • 0032553439 scopus 로고    scopus 로고
    • SRC-1 and GRIP1 coactivate transcription with hepatocyte nuclear factor 4
    • Wang J.C., Stafford J.M., and Granner D.K. SRC-1 and GRIP1 coactivate transcription with hepatocyte nuclear factor 4. J. Biol. Chem. 273 (1998) 30847-30850
    • (1998) J. Biol. Chem. , vol.273 , pp. 30847-30850
    • Wang, J.C.1    Stafford, J.M.2    Granner, D.K.3
  • 38
    • 0038241793 scopus 로고    scopus 로고
    • HNF4: a central regulator of hepatocyte differentiation and function
    • Watt A.J., Garrison W.D., and Duncan S.A. HNF4: a central regulator of hepatocyte differentiation and function. Hepatology 37 (2003) 1249-1253
    • (2003) Hepatology , vol.37 , pp. 1249-1253
    • Watt, A.J.1    Garrison, W.D.2    Duncan, S.A.3
  • 40
    • 0042334873 scopus 로고    scopus 로고
    • Review of the in vivo functions of the p160 steroid receptor coactivator family
    • Xu J., and Li Q. Review of the in vivo functions of the p160 steroid receptor coactivator family. Mol. Endocrinol. 17 (2003) 1681-1692
    • (2003) Mol. Endocrinol. , vol.17 , pp. 1681-1692
    • Xu, J.1    Li, Q.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.