Id helix–loop–helix proteins inhibit nucleoprotein complex formation by the TCF ETS‐domain transcription factors
Abstract The Id subfamily of helix–loop–helix (HLH) proteins plays a fundamental role in the regulation of cellular proliferation and differentiation. Id proteins are thought to inhibit differentiation mainly through interaction with other HLH proteins and by blocking their DNA‐binding activity. Mem...
Ausführliche Beschreibung
Autor*in: |
Yates, Paula R. [verfasserIn] Atherton, Graham T. [verfasserIn] Deed, Richard W. [verfasserIn] Norton, John D. [verfasserIn] Sharrocks, Andrew D. [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
1999 |
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Schlagwörter: |
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Anmerkung: |
© European Molecular Biology Organization 1999 |
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Übergeordnetes Werk: |
Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 18(1999), 4 vom: 15. Feb., Seite 968-976 |
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Übergeordnetes Werk: |
volume:18 ; year:1999 ; number:4 ; day:15 ; month:02 ; pages:968-976 |
Links: |
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DOI / URN: |
10.1093/emboj/18.4.968 |
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Katalog-ID: |
SPR058003134 |
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100 | 1 | |a Yates, Paula R. |e verfasserin |4 aut | |
245 | 1 | 0 | |a Id helix–loop–helix proteins inhibit nucleoprotein complex formation by the TCF ETS‐domain transcription factors |
264 | 1 | |c 1999 | |
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520 | |a Abstract The Id subfamily of helix–loop–helix (HLH) proteins plays a fundamental role in the regulation of cellular proliferation and differentiation. Id proteins are thought to inhibit differentiation mainly through interaction with other HLH proteins and by blocking their DNA‐binding activity. Members of the ternary complex factor (TCF) subfamily of ETS‐domain proteins have key functions in regulating immediate‐early gene expression in response to mitogenic stimulation. TCFs form DNA‐bound complexes with the serum response factor (SRF) and are direct targets of MAP kinase (MAPK) signal transduction cascades. In this study we demonstrate functional interactions between Id proteins and TCFs. Ids bind to the ETS DNA‐binding domain and disrupt the formation of DNA‐bound complexes between TCFs and SRF on the c‐fos serum response element (SRE). Inhibition occurs by disrupting protein–DNA interactions with the TCF component of this complex. In vivo, the Id proteins cause down‐regulation of the transcriptional activity mediated by the TCFs and thereby block MAPK signalling to SREs. Therefore, our results demonstrate a novel facet of Id function in the coordination of mitogenic signalling and cell cycle entry. | ||
650 | 4 | |a ETS‐domain proteins |7 (dpeaa)DE-He213 | |
650 | 4 | |a helix–loop–helix proteins |7 (dpeaa)DE-He213 | |
650 | 4 | |a Ids |7 (dpeaa)DE-He213 | |
650 | 4 | |a TCFs |7 (dpeaa)DE-He213 | |
650 | 4 | |a transcription factor |7 (dpeaa)DE-He213 | |
700 | 1 | |a Atherton, Graham T. |e verfasserin |4 aut | |
700 | 1 | |a Deed, Richard W. |e verfasserin |4 aut | |
700 | 1 | |a Norton, John D. |e verfasserin |4 aut | |
700 | 1 | |a Sharrocks, Andrew D. |e verfasserin |4 aut | |
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1999 |
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10.1093/emboj/18.4.968 doi (DE-627)SPR058003134 (SPR)18.4.968-e DE-627 ger DE-627 rakwb eng Yates, Paula R. verfasserin aut Id helix–loop–helix proteins inhibit nucleoprotein complex formation by the TCF ETS‐domain transcription factors 1999 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1999 Abstract The Id subfamily of helix–loop–helix (HLH) proteins plays a fundamental role in the regulation of cellular proliferation and differentiation. Id proteins are thought to inhibit differentiation mainly through interaction with other HLH proteins and by blocking their DNA‐binding activity. Members of the ternary complex factor (TCF) subfamily of ETS‐domain proteins have key functions in regulating immediate‐early gene expression in response to mitogenic stimulation. TCFs form DNA‐bound complexes with the serum response factor (SRF) and are direct targets of MAP kinase (MAPK) signal transduction cascades. In this study we demonstrate functional interactions between Id proteins and TCFs. Ids bind to the ETS DNA‐binding domain and disrupt the formation of DNA‐bound complexes between TCFs and SRF on the c‐fos serum response element (SRE). Inhibition occurs by disrupting protein–DNA interactions with the TCF component of this complex. In vivo, the Id proteins cause down‐regulation of the transcriptional activity mediated by the TCFs and thereby block MAPK signalling to SREs. Therefore, our results demonstrate a novel facet of Id function in the coordination of mitogenic signalling and cell cycle entry. ETS‐domain proteins (dpeaa)DE-He213 helix–loop–helix proteins (dpeaa)DE-He213 Ids (dpeaa)DE-He213 TCFs (dpeaa)DE-He213 transcription factor (dpeaa)DE-He213 Atherton, Graham T. verfasserin aut Deed, Richard W. verfasserin aut Norton, John D. verfasserin aut Sharrocks, Andrew D. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 18(1999), 4 vom: 15. Feb., Seite 968-976 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:18 year:1999 number:4 day:15 month:02 pages:968-976 https://dx.doi.org/10.1093/emboj/18.4.968 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 18 1999 4 15 02 968-976 |
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10.1093/emboj/18.4.968 doi (DE-627)SPR058003134 (SPR)18.4.968-e DE-627 ger DE-627 rakwb eng Yates, Paula R. verfasserin aut Id helix–loop–helix proteins inhibit nucleoprotein complex formation by the TCF ETS‐domain transcription factors 1999 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1999 Abstract The Id subfamily of helix–loop–helix (HLH) proteins plays a fundamental role in the regulation of cellular proliferation and differentiation. Id proteins are thought to inhibit differentiation mainly through interaction with other HLH proteins and by blocking their DNA‐binding activity. Members of the ternary complex factor (TCF) subfamily of ETS‐domain proteins have key functions in regulating immediate‐early gene expression in response to mitogenic stimulation. TCFs form DNA‐bound complexes with the serum response factor (SRF) and are direct targets of MAP kinase (MAPK) signal transduction cascades. In this study we demonstrate functional interactions between Id proteins and TCFs. Ids bind to the ETS DNA‐binding domain and disrupt the formation of DNA‐bound complexes between TCFs and SRF on the c‐fos serum response element (SRE). Inhibition occurs by disrupting protein–DNA interactions with the TCF component of this complex. In vivo, the Id proteins cause down‐regulation of the transcriptional activity mediated by the TCFs and thereby block MAPK signalling to SREs. Therefore, our results demonstrate a novel facet of Id function in the coordination of mitogenic signalling and cell cycle entry. ETS‐domain proteins (dpeaa)DE-He213 helix–loop–helix proteins (dpeaa)DE-He213 Ids (dpeaa)DE-He213 TCFs (dpeaa)DE-He213 transcription factor (dpeaa)DE-He213 Atherton, Graham T. verfasserin aut Deed, Richard W. verfasserin aut Norton, John D. verfasserin aut Sharrocks, Andrew D. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 18(1999), 4 vom: 15. Feb., Seite 968-976 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:18 year:1999 number:4 day:15 month:02 pages:968-976 https://dx.doi.org/10.1093/emboj/18.4.968 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 18 1999 4 15 02 968-976 |
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10.1093/emboj/18.4.968 doi (DE-627)SPR058003134 (SPR)18.4.968-e DE-627 ger DE-627 rakwb eng Yates, Paula R. verfasserin aut Id helix–loop–helix proteins inhibit nucleoprotein complex formation by the TCF ETS‐domain transcription factors 1999 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1999 Abstract The Id subfamily of helix–loop–helix (HLH) proteins plays a fundamental role in the regulation of cellular proliferation and differentiation. Id proteins are thought to inhibit differentiation mainly through interaction with other HLH proteins and by blocking their DNA‐binding activity. Members of the ternary complex factor (TCF) subfamily of ETS‐domain proteins have key functions in regulating immediate‐early gene expression in response to mitogenic stimulation. TCFs form DNA‐bound complexes with the serum response factor (SRF) and are direct targets of MAP kinase (MAPK) signal transduction cascades. In this study we demonstrate functional interactions between Id proteins and TCFs. Ids bind to the ETS DNA‐binding domain and disrupt the formation of DNA‐bound complexes between TCFs and SRF on the c‐fos serum response element (SRE). Inhibition occurs by disrupting protein–DNA interactions with the TCF component of this complex. In vivo, the Id proteins cause down‐regulation of the transcriptional activity mediated by the TCFs and thereby block MAPK signalling to SREs. Therefore, our results demonstrate a novel facet of Id function in the coordination of mitogenic signalling and cell cycle entry. ETS‐domain proteins (dpeaa)DE-He213 helix–loop–helix proteins (dpeaa)DE-He213 Ids (dpeaa)DE-He213 TCFs (dpeaa)DE-He213 transcription factor (dpeaa)DE-He213 Atherton, Graham T. verfasserin aut Deed, Richard W. verfasserin aut Norton, John D. verfasserin aut Sharrocks, Andrew D. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 18(1999), 4 vom: 15. Feb., Seite 968-976 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:18 year:1999 number:4 day:15 month:02 pages:968-976 https://dx.doi.org/10.1093/emboj/18.4.968 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 18 1999 4 15 02 968-976 |
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10.1093/emboj/18.4.968 doi (DE-627)SPR058003134 (SPR)18.4.968-e DE-627 ger DE-627 rakwb eng Yates, Paula R. verfasserin aut Id helix–loop–helix proteins inhibit nucleoprotein complex formation by the TCF ETS‐domain transcription factors 1999 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1999 Abstract The Id subfamily of helix–loop–helix (HLH) proteins plays a fundamental role in the regulation of cellular proliferation and differentiation. Id proteins are thought to inhibit differentiation mainly through interaction with other HLH proteins and by blocking their DNA‐binding activity. Members of the ternary complex factor (TCF) subfamily of ETS‐domain proteins have key functions in regulating immediate‐early gene expression in response to mitogenic stimulation. TCFs form DNA‐bound complexes with the serum response factor (SRF) and are direct targets of MAP kinase (MAPK) signal transduction cascades. In this study we demonstrate functional interactions between Id proteins and TCFs. Ids bind to the ETS DNA‐binding domain and disrupt the formation of DNA‐bound complexes between TCFs and SRF on the c‐fos serum response element (SRE). Inhibition occurs by disrupting protein–DNA interactions with the TCF component of this complex. In vivo, the Id proteins cause down‐regulation of the transcriptional activity mediated by the TCFs and thereby block MAPK signalling to SREs. Therefore, our results demonstrate a novel facet of Id function in the coordination of mitogenic signalling and cell cycle entry. ETS‐domain proteins (dpeaa)DE-He213 helix–loop–helix proteins (dpeaa)DE-He213 Ids (dpeaa)DE-He213 TCFs (dpeaa)DE-He213 transcription factor (dpeaa)DE-He213 Atherton, Graham T. verfasserin aut Deed, Richard W. verfasserin aut Norton, John D. verfasserin aut Sharrocks, Andrew D. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 18(1999), 4 vom: 15. Feb., Seite 968-976 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:18 year:1999 number:4 day:15 month:02 pages:968-976 https://dx.doi.org/10.1093/emboj/18.4.968 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 18 1999 4 15 02 968-976 |
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10.1093/emboj/18.4.968 doi (DE-627)SPR058003134 (SPR)18.4.968-e DE-627 ger DE-627 rakwb eng Yates, Paula R. verfasserin aut Id helix–loop–helix proteins inhibit nucleoprotein complex formation by the TCF ETS‐domain transcription factors 1999 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 1999 Abstract The Id subfamily of helix–loop–helix (HLH) proteins plays a fundamental role in the regulation of cellular proliferation and differentiation. Id proteins are thought to inhibit differentiation mainly through interaction with other HLH proteins and by blocking their DNA‐binding activity. Members of the ternary complex factor (TCF) subfamily of ETS‐domain proteins have key functions in regulating immediate‐early gene expression in response to mitogenic stimulation. TCFs form DNA‐bound complexes with the serum response factor (SRF) and are direct targets of MAP kinase (MAPK) signal transduction cascades. In this study we demonstrate functional interactions between Id proteins and TCFs. Ids bind to the ETS DNA‐binding domain and disrupt the formation of DNA‐bound complexes between TCFs and SRF on the c‐fos serum response element (SRE). Inhibition occurs by disrupting protein–DNA interactions with the TCF component of this complex. In vivo, the Id proteins cause down‐regulation of the transcriptional activity mediated by the TCFs and thereby block MAPK signalling to SREs. Therefore, our results demonstrate a novel facet of Id function in the coordination of mitogenic signalling and cell cycle entry. ETS‐domain proteins (dpeaa)DE-He213 helix–loop–helix proteins (dpeaa)DE-He213 Ids (dpeaa)DE-He213 TCFs (dpeaa)DE-He213 transcription factor (dpeaa)DE-He213 Atherton, Graham T. verfasserin aut Deed, Richard W. verfasserin aut Norton, John D. verfasserin aut Sharrocks, Andrew D. verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 18(1999), 4 vom: 15. Feb., Seite 968-976 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:18 year:1999 number:4 day:15 month:02 pages:968-976 https://dx.doi.org/10.1093/emboj/18.4.968 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4116 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4311 GBV_ILN_4313 GBV_ILN_4314 GBV_ILN_4318 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4598 GBV_ILN_4700 AR 18 1999 4 15 02 968-976 |
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Enthalten in The EMBO Journal 18(1999), 4 vom: 15. Feb., Seite 968-976 volume:18 year:1999 number:4 day:15 month:02 pages:968-976 |
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Yates, Paula R. @@aut@@ Atherton, Graham T. @@aut@@ Deed, Richard W. @@aut@@ Norton, John D. @@aut@@ Sharrocks, Andrew D. @@aut@@ |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000naa a22002652 4500</leader><controlfield tag="001">SPR058003134</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20241024065049.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">241024s1999 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1093/emboj/18.4.968</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR058003134</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)18.4.968-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Yates, Paula R.</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Id helix–loop–helix proteins inhibit nucleoprotein complex formation by the TCF ETS‐domain transcription factors</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1999</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© European Molecular Biology Organization 1999</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract The Id subfamily of helix–loop–helix (HLH) proteins plays a fundamental role in the regulation of cellular proliferation and differentiation. Id proteins are thought to inhibit differentiation mainly through interaction with other HLH proteins and by blocking their DNA‐binding activity. Members of the ternary complex factor (TCF) subfamily of ETS‐domain proteins have key functions in regulating immediate‐early gene expression in response to mitogenic stimulation. TCFs form DNA‐bound complexes with the serum response factor (SRF) and are direct targets of MAP kinase (MAPK) signal transduction cascades. In this study we demonstrate functional interactions between Id proteins and TCFs. Ids bind to the ETS DNA‐binding domain and disrupt the formation of DNA‐bound complexes between TCFs and SRF on the c‐fos serum response element (SRE). Inhibition occurs by disrupting protein–DNA interactions with the TCF component of this complex. In vivo, the Id proteins cause down‐regulation of the transcriptional activity mediated by the TCFs and thereby block MAPK signalling to SREs. 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Yates, Paula R. |
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Yates, Paula R. misc ETS‐domain proteins misc helix–loop–helix proteins misc Ids misc TCFs misc transcription factor Id helix–loop–helix proteins inhibit nucleoprotein complex formation by the TCF ETS‐domain transcription factors |
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Id helix–loop–helix proteins inhibit nucleoprotein complex formation by the TCF ETS‐domain transcription factors ETS‐domain proteins (dpeaa)DE-He213 helix–loop–helix proteins (dpeaa)DE-He213 Ids (dpeaa)DE-He213 TCFs (dpeaa)DE-He213 transcription factor (dpeaa)DE-He213 |
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misc ETS‐domain proteins misc helix–loop–helix proteins misc Ids misc TCFs misc transcription factor |
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Id helix–loop–helix proteins inhibit nucleoprotein complex formation by the TCF ETS‐domain transcription factors |
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Id helix–loop–helix proteins inhibit nucleoprotein complex formation by the TCF ETS‐domain transcription factors |
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id helix–loop–helix proteins inhibit nucleoprotein complex formation by the tcf ets‐domain transcription factors |
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Id helix–loop–helix proteins inhibit nucleoprotein complex formation by the TCF ETS‐domain transcription factors |
abstract |
Abstract The Id subfamily of helix–loop–helix (HLH) proteins plays a fundamental role in the regulation of cellular proliferation and differentiation. Id proteins are thought to inhibit differentiation mainly through interaction with other HLH proteins and by blocking their DNA‐binding activity. Members of the ternary complex factor (TCF) subfamily of ETS‐domain proteins have key functions in regulating immediate‐early gene expression in response to mitogenic stimulation. TCFs form DNA‐bound complexes with the serum response factor (SRF) and are direct targets of MAP kinase (MAPK) signal transduction cascades. In this study we demonstrate functional interactions between Id proteins and TCFs. Ids bind to the ETS DNA‐binding domain and disrupt the formation of DNA‐bound complexes between TCFs and SRF on the c‐fos serum response element (SRE). Inhibition occurs by disrupting protein–DNA interactions with the TCF component of this complex. In vivo, the Id proteins cause down‐regulation of the transcriptional activity mediated by the TCFs and thereby block MAPK signalling to SREs. Therefore, our results demonstrate a novel facet of Id function in the coordination of mitogenic signalling and cell cycle entry. © European Molecular Biology Organization 1999 |
abstractGer |
Abstract The Id subfamily of helix–loop–helix (HLH) proteins plays a fundamental role in the regulation of cellular proliferation and differentiation. Id proteins are thought to inhibit differentiation mainly through interaction with other HLH proteins and by blocking their DNA‐binding activity. Members of the ternary complex factor (TCF) subfamily of ETS‐domain proteins have key functions in regulating immediate‐early gene expression in response to mitogenic stimulation. TCFs form DNA‐bound complexes with the serum response factor (SRF) and are direct targets of MAP kinase (MAPK) signal transduction cascades. In this study we demonstrate functional interactions between Id proteins and TCFs. Ids bind to the ETS DNA‐binding domain and disrupt the formation of DNA‐bound complexes between TCFs and SRF on the c‐fos serum response element (SRE). Inhibition occurs by disrupting protein–DNA interactions with the TCF component of this complex. In vivo, the Id proteins cause down‐regulation of the transcriptional activity mediated by the TCFs and thereby block MAPK signalling to SREs. Therefore, our results demonstrate a novel facet of Id function in the coordination of mitogenic signalling and cell cycle entry. © European Molecular Biology Organization 1999 |
abstract_unstemmed |
Abstract The Id subfamily of helix–loop–helix (HLH) proteins plays a fundamental role in the regulation of cellular proliferation and differentiation. Id proteins are thought to inhibit differentiation mainly through interaction with other HLH proteins and by blocking their DNA‐binding activity. Members of the ternary complex factor (TCF) subfamily of ETS‐domain proteins have key functions in regulating immediate‐early gene expression in response to mitogenic stimulation. TCFs form DNA‐bound complexes with the serum response factor (SRF) and are direct targets of MAP kinase (MAPK) signal transduction cascades. In this study we demonstrate functional interactions between Id proteins and TCFs. Ids bind to the ETS DNA‐binding domain and disrupt the formation of DNA‐bound complexes between TCFs and SRF on the c‐fos serum response element (SRE). Inhibition occurs by disrupting protein–DNA interactions with the TCF component of this complex. In vivo, the Id proteins cause down‐regulation of the transcriptional activity mediated by the TCFs and thereby block MAPK signalling to SREs. Therefore, our results demonstrate a novel facet of Id function in the coordination of mitogenic signalling and cell cycle entry. © European Molecular Biology Organization 1999 |
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container_issue |
4 |
title_short |
Id helix–loop–helix proteins inhibit nucleoprotein complex formation by the TCF ETS‐domain transcription factors |
url |
https://dx.doi.org/10.1093/emboj/18.4.968 |
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author2 |
Atherton, Graham T. Deed, Richard W. Norton, John D. Sharrocks, Andrew D. |
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doi_str |
10.1093/emboj/18.4.968 |
up_date |
2024-10-24T04:55:38.533Z |
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|
score |
7.402815 |