DOI: 10.1126/science.279.5351.700. Differential Use of CREB Binding Protein-Coactivator Complexes

Differential Use of CREB Binding Protein-Coactivator Complexes

10.1126/science.279.5351.700

Crossref journal-article

American Association for the Advancement of Science (AAAS)

Science (221)

Abstract

CREB binding protein (CBP) functions as an essential coactivator of transcription factors that are inhibited by the adenovirus early gene product E1A. Transcriptional activation by the signal transducer and activator of transcription–1 (STAT1) protein requires the C/H3 domain in CBP, which is the primary target of E1A inhibition. Here it was found that the C/H3 domain is not required for retinoic acid receptor (RAR) function, nor is it involved in E1A inhibition. Instead, E1A inhibits RAR function by preventing the assembly of CBP–nuclear receptor coactivator complexes, revealing differences in required CBP domains for transcriptional activation by RAR and STAT1.

Bibliography

Kurokawa, R., Kalafus, D., Ogliastro, M.-H., Kioussi, C., Xu, L., Torchia, J., Rosenfeld, M. G., & Glass, C. K. (1998). Differential Use of CREB Binding Protein-Coactivator Complexes. Science, 279(5351), 700â703.

Authors 8

Riki Kurokawa (first)
Daniel Kalafus (additional)
Marie-Hélène Ogliastro (additional)
Chrissa Kioussi (additional)
Lan Xu (additional)
Joseph Torchia (additional)
Michael G. Rosenfeld (additional)
Christopher K. Glass (additional)

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We thank T. Schneiderman for assistance with preparation of the manuscript. D.K. is supported by a predoctoral training grant from the National Cancer Institute J.T. by the National Cancer Institute of Canada L.X. by an American Heart Association predoctoral fellowship and M.-H.O. by the National Institute of Agronomical Research France. M.G.R. is an Investigator of the Howard Hughes Medical Institute. C.K.G. is an Established Investigator of the American Heart Association. Supported by grants from NIH to M.G.R. and C.K.G.

Dates

Type	When
Created	23 years, 1 month ago (July 27, 2002, 5:42 a.m.)
Deposited	1 year, 7 months ago (Jan. 13, 2024, 12:57 a.m.)
Indexed	1 month, 4 weeks ago (July 2, 2025, 2:45 p.m.)
Issued	27 years, 7 months ago (Jan. 30, 1998)
Published	27 years, 7 months ago (Jan. 30, 1998)
Published Print	27 years, 7 months ago (Jan. 30, 1998)

Funders 0

None

BibTeX

@article{Kurokawa_1998, title={Differential Use of CREB Binding Protein-Coactivator Complexes}, volume={279}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.279.5351.700}, DOI={10.1126/science.279.5351.700}, number={5351}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Kurokawa, Riki and Kalafus, Daniel and Ogliastro, Marie-Hélène and Kioussi, Chrissa and Xu, Lan and Torchia, Joseph and Rosenfeld, Michael G. and Glass, Christopher K.}, year={1998}, month=jan, pages={700–703} }

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      "year": "1996",
      "unstructured": "Kamei Y., et al., Cell 85, 403 (1996).",
      "journal-title": "Cell"
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    {
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      "doi-asserted-by": "crossref",
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    {
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      "doi-asserted-by": "crossref",
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      "doi-asserted-by": "crossref",
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    {
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      "doi-asserted-by": "crossref",
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      "unstructured": "Nakajima T., Uchida C., Anderson S. F., Parvin J. D., Montminy M., Genes Dev. 11, 738 (1997);",
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    {
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    {
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      "unstructured": "Mutations in CBP and E1A were generated with the polymerase chain reaction. Small regions spanning each deletion or point mutation were confirmed by sequence analysis and transferred into the wild-type cDNA backbone. At least two independent clones of each mutant were analyzed for expression and function. For transient transfection assays of CBP and E1A function we plated CV1 or HeLa cells in 24-well plates and transfected them with luciferase reporter genes and CBP or E1A expression vectors using CaPO 4 (19). Salmon sperm DNA was used as a carrier to balance the total amount of transfected DNA. Cells were treated with the RAR-specific ligand TTNPB {(E)-4-[2-(5 5 8 8-tetramethyl-5 6 7 8-tetrahydro-2-napthalenyl)-1-propenyl] benzoic acid} (0.1 \u03bcM) or interferon-\u03b3 (100 u/ml) for 24 hours or 6 hours respectively before determination of luciferase activity."
    },
    {
      "key": "e_1_3_1_11_2",
      "unstructured": "R. Kurokawa and D. Kalafus unpublished data."
    },
    {
      "key": "e_1_3_1_12_2",
      "unstructured": "Full-length CBP and CBP\u0394C/H3 were expressed in SF9 cells with a baculovirus vector and contained a COOH-terminal FLAG epitope which permitted purification on a matrix of FLAG antibody. GST fusion proteins were expressed in Escherichia coli and purified on a glutathione agarose affinity matrix. In studies with full-length CBP SF9 whole-cell extracts containing FLAG-tagged CBP were incubated with GST-E1A fusion proteins produced in bacteria and captured on a glutathione affinity matrix. After they were washed protein complexes were resolved by SDS\u2013polyacrylamide gel electrophoresis (SDS-PAGE) and analyzed by protein immunoblotting with a monoclonal antibody to FLAG. In studies examining the interaction of p/CIP and E1A with specific domains of CBP [ 35 S]p/CIP or [ 35 S]E1A proteins were produced by translation in vitro and incubated with GST-CBP fusion proteins. After they were extensively washed specifically bound proteins were resolved by SDS-PAGE and detected by autoradiography. For Far Western analysis of E1A-CBP interactions 12 S E1A and 13 S E1A cDNAs were introduced into a vector providing an in-frame phosphorylation site for protein kinase A. After phosphorylation with 32 P radiolabeled 12 S E1A and 13 S E1A were used to probe nitrocellulose membranes containing CBP fragments as previously described (12)."
    },
    {
      "key": "e_1_3_1_13_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.8197458"
    },
    {
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    {
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    {
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      "unstructured": "; H. Hong K. Kohli A. Trivedi D. L. Johnson M. R. Stallcup ibid. p. 4948; H. Chen et al. Cell 90 569 (1997);"
    },
    {
      "key": "e_1_3_1_14_6",
      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.277.5328.965"
    },
    {
      "key": "e_1_3_1_15_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1038/42652"
    },
    {
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      "doi-asserted-by": "crossref",
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      "DOI": "10.1128/jvi.67.1.476-488.1993",
      "volume": "67",
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      "unstructured": "Wang H.-G. H., et al., J. Virol. 67, 476 (1993).",
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    {
      "key": "e_1_3_1_17_2",
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      "first-page": "165",
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      "volume": "299",
      "author": "McBurney M. W.",
      "year": "1982",
      "unstructured": "McBurney M. W., Jones-Villeneuve E. M. V., Edwards M. K. S., Anderson P. J., Nature 299, 165 (1982).",
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    },
    {
      "key": "e_1_3_1_18_2",
      "unstructured": "To assess the effects of E1A mutants on retinoic acid\u2013dependent differentiation of P19 cells we cotransfected human kidney carcinoma 293 cells with 1.5 \u03bcg per 6-cm dish of pCL-7 helper-free retroviral packaging vector and pCL1-E1A pCL1-H3N and pCL1 vector as indicated using the CaPO 4 method. Media was changed 8 hours after transfection. After 12 hours the supernatant was used in 1:100 dilution for infecting P19 cells. Retroviral vectors and packaging plasmids that produce helper-free retrovirus with 1 \u00d7 10 6 \u2009to\u20095 \u00d7 10 6 titers (19) were used for E1A and H3N overexpression. The supernatant of 293 cells infected with pCL-7 pCL1-E1A or pCL1-H3N packaging constructs were used to infect P19 cells for 2 days. P19 cells were induced to differentiate with 0.5 \u03bcM retinoic acid in bacterial-grade petri dishes. Two days after infection and aggregation in the presence of retinoic acid embryoid bodies were collected and plated again in bacterial-grade petri dishes in the absence of virus. Two days later cells were transferred to poly- l -lysine\u2013coated glass cover slips in media without retinoic acid (19). After 2 to 3 days cells were fixed with 4% formaldehyde and prepared for immunohistochemistry. Rabbit polyclonal antibodies to NF (Sigma) were diluted 1:100 in 0.5% blocking buffer (Boehringer Mannheim). Detection antibody fluorescein isothiocyanate\u2013conjugated to goat antibody to rabbit F(ab) 2 fragments was used in 1:100 dilution. Fixed P19 cells were incubated with antibodies to NF for 2 hours  at room temperature and rinsed before applying secondary antibody for two more hours at room temperature. Immunofluoresence-stained preparations were viewed with a Zeiss Axiophot photomicroscope. Photographic prints referring to comparative immunostaining were prepared under identical conditions."
    },
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      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.279.5351.703"
    },
    {
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      "doi-asserted-by": "crossref",
      "first-page": "528",
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      "volume": "371",
      "author": "Kurokawa R.",
      "year": "1994",
      "unstructured": "Kurokawa R., et al., Nature 371, 528 (1994);",
      "journal-title": "Nature"
    },
    {
      "key": "e_1_3_1_20_3",
      "doi-asserted-by": "publisher",
      "DOI": "10.1128/jvi.70.8.5701-5705.1996"
    },
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      "key": "e_1_3_1_21_2",
      "unstructured": "We thank T. Schneiderman for assistance with preparation of the manuscript. D.K. is supported by a predoctoral training grant from the National Cancer Institute J.T. by the National Cancer Institute of Canada L.X. by an American Heart Association predoctoral fellowship and M.-H.O. by the National Institute of Agronomical Research France. M.G.R. is an Investigator of the Howard Hughes Medical Institute. C.K.G. is an Established Investigator of the American Heart Association. Supported by grants from NIH to M.G.R. and C.K.G."
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