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Research article

Co-activator SRC-1 is dispensable for transcriptional control by STAT3

Helena Cvijic, Kay Bauer, Dennis Löffler, Gabriele Pfeifer, Conny Blumert, Antje K. Kretzschmar, Christian Henze, Katja Brocke-Heidrich, Friedemann Horn
Biochemical Journal May 15, 2009, 420 (1) 123-132; DOI: 10.1042/BJ20081989
Helena Cvijic
Institute of Clinical Immunology and Transfusion Medicine, University of Leipzig, Johannisallee 30, 04103 Leipzig, Germany
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Kay Bauer
Institute of Clinical Immunology and Transfusion Medicine, University of Leipzig, Johannisallee 30, 04103 Leipzig, Germany
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Dennis Löffler
Institute of Clinical Immunology and Transfusion Medicine, University of Leipzig, Johannisallee 30, 04103 Leipzig, Germany
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Gabriele Pfeifer
Institute of Clinical Immunology and Transfusion Medicine, University of Leipzig, Johannisallee 30, 04103 Leipzig, Germany
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Conny Blumert
Institute of Clinical Immunology and Transfusion Medicine, University of Leipzig, Johannisallee 30, 04103 Leipzig, Germany
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Antje K. Kretzschmar
Institute of Clinical Immunology and Transfusion Medicine, University of Leipzig, Johannisallee 30, 04103 Leipzig, Germany
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Christian Henze
Institute of Clinical Immunology and Transfusion Medicine, University of Leipzig, Johannisallee 30, 04103 Leipzig, Germany
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Katja Brocke-Heidrich
Institute of Clinical Immunology and Transfusion Medicine, University of Leipzig, Johannisallee 30, 04103 Leipzig, Germany
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Friedemann Horn
Institute of Clinical Immunology and Transfusion Medicine, University of Leipzig, Johannisallee 30, 04103 Leipzig, Germany
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  • For correspondence: friedemann.horn@medizin.uni-leipzig.de
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Abstract

SRC (steroid receptor co-activator)-1 has been reported to interact with and to be an essential co-activator for several members of the STAT (signal transducer and activator of transcription) family, including STAT3, the major signal transducer of IL (interleukin)-6. We addressed the question of whether SRC-1 is crucial for IL-6- and STAT3-mediated physiological responses such as myeloma cell survival and acute-phase protein induction. In fact, silencing of SRC-1 by RNA interference rapidly induced apoptosis in IL-6-dependent INA-6 human myeloma cells, comparable with what was observed upon silencing of STAT3. Using chromatin immunoprecipitation at STAT3 target regions of various genes, however, we observed constitutive binding of SRC-1 that decreased when INA-6 cells were treated with IL-6. The same held true for STAT3 target genes analysed in HepG2 human hepatocellular carcinoma cells. SRC-1-knockdown studies demonstrated that STAT3-controlled promoters require neither SRC-1 nor the other p160 family members SRC-2 or SRC-3 in HepG2 cells. Furthermore, microarray expression profiling demonstrated that the responsiveness of IL-6 target genes is not affected by SRC-1 silencing. In contrast, co-activators of the CBP [CREB (cAMP-response element-binding protein)-binding protein]/p300 family proved functionally important for the transactivation potential of STAT3 and bound inducibly to STAT3 target regions. This recruitment did not depend on the presence of SRC-1. Altogether, this suggests that functional impairment of STAT3 is not involved in the induction of myeloma cell apoptosis by SRC-1 silencing. We therefore conclude that STAT3 transactivates its target genes by the recruitment of CBP/p300 co-activators and that this process generally does not require the contribution of SRC-1.

  • acute-phase reaction
  • interleukin-6 (IL-6)
  • signal transducer and activator of transcription 3 (STAT3)
  • steroid receptor co-activator-1 (SRC-1)
  • transcription control

Abbreviations: ACT, α1-antichymotrypsin; ChIP, chromatin immunoprecipitation; CREB, cAMP-response element-binding protein; CBP, CREB-binding protein; Crif1, CR6-interacting factor 1; DMEM, Dulbecco's modified minimal essential medium; EGFP, enhanced green fluorescent protein; ERK, extracellular-signal-regulated kinase; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; gp, glycoprotein; GRIP-1, glutamate receptor-interacting protein 1; HEK, human embryonic kidney; IL, interleukin; IκBα, inhibitor of nuclear factor κB α; NCoA, nuclear receptor co-activator; NF-κB, nuclear factor κB; p/CAF, p300/CBP-associated factor; RNAi, RNA interference; shRNA, small hairpin RNA; SOCS3, suppressor of cytokine signalling 3; SRC, steroid receptor co-activator; STAT, signal transducer and activator of transcription; TRAP220, thyroid hormone receptor-associated polypeptide 220

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May 2009

Volume: 420 Issue: 1

Biochemical Journal: 420 (1)
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Co-activator SRC-1 is dispensable for transcriptional control by STAT3
Helena Cvijic, Kay Bauer, Dennis Löffler, Gabriele Pfeifer, Conny Blumert, Antje K. Kretzschmar, Christian Henze, Katja Brocke-Heidrich, Friedemann Horn
Biochemical Journal May 2009, 420 (1) 123-132; DOI: 10.1042/BJ20081989
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Co-activator SRC-1 is dispensable for transcriptional control by STAT3
Helena Cvijic, Kay Bauer, Dennis Löffler, Gabriele Pfeifer, Conny Blumert, Antje K. Kretzschmar, Christian Henze, Katja Brocke-Heidrich, Friedemann Horn
Biochemical Journal May 2009, 420 (1) 123-132; DOI: 10.1042/BJ20081989

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Keywords

acute-phase reaction
interleukin-6 (IL-6)
signal transducer and activator of transcription 3 (STAT3)
steroid receptor co-activator-1 (SRC-1)
transcription control

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