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Novel isoforms of the TFIID subunit TAF4 modulate nuclear receptor-mediated transcriptional activity

Academic Article
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Overview

authors

  • Brunkhorst, A.
  • Neuman, T.
  • Hall, A.
  • Arenas, E.
  • Bartfai, Tamas
  • Hermanson, O.
  • Metsis, Madis

publication date

  • December 2004

journal

  • Biochemical and Biophysical Research Communications  Journal

abstract

  • The transcription factor TFIID consists of TATA-binding protein (TBP) and TBP-associated factors (TAFs). TAFs are essential for modulation of transcriptional activity but the regulation of TAFs is complex and many important aspects remain unclear. In this study, we have identified and characterized five novel truncated forms of the TFIID subunit TAF4 (TAF(II)135). Analysis of the mouse gene structure revealed that all truncations were the results of alternative splicing and resulted in the loss of domains or parts of domains implicated in TAF4 functional interactions. Results from transcriptional assays showed that several of the TAF4 isoforms exerted dominant negative effects on TAF4 activity in nuclear receptor-mediated transcriptional activation. In addition, alternative TAF4 isoforms could be detected in specific cell types. Our results indicate an additional level of complexity in TAF4-mediated regulation of transcription and suggest context-specific roles for these new TAF4 isoforms in transcriptional regulation in vivo.

subject areas

  • Alternative Splicing
  • Animals
  • Brain
  • COS Cells
  • Cells, Cultured
  • Cercopithecus aethiops
  • Cyclic AMP
  • Cyclic AMP Response Element-Binding Protein
  • Gene Deletion
  • Gene Expression
  • Genome Components
  • Mice
  • Mice, Inbred BALB C
  • Neurons
  • Protein Isoforms
  • Protein Subunits
  • Receptors, Retinoic Acid
  • TATA-Binding Protein Associated Factors
  • Transcription Factor TFIID
  • Transcription, Genetic
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Research

keywords

  • CREB
  • TAFII135
  • alternative splicing
  • dTAFII110
  • neuronal
  • retinoic acid receptor
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Identity

International Standard Serial Number (ISSN)

  • 0006-291X

Digital Object Identifier (DOI)

  • 10.1016/j.bbrc.2004.10.078

PubMed ID

  • 15530431
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Additional Document Info

start page

  • 574

end page

  • 579

volume

  • 325

issue

  • 2

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