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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenovirus E1A Proteins / metabolism*
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Adenovirus E1A Proteins / pharmacology
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Animals
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Binding Sites
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CREB-Binding Protein
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Cell Differentiation
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Cell Line
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DNA-Binding Proteins / metabolism
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Histone Acetyltransferases
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Humans
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Mutation
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Nuclear Proteins / chemistry
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Nuclear Proteins / genetics
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Nuclear Proteins / metabolism*
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Nuclear Receptor Coactivator 1
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Nuclear Receptor Coactivator 3
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Protein Binding
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Receptors, Retinoic Acid / metabolism
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Recombinant Fusion Proteins / metabolism
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STAT1 Transcription Factor
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Trans-Activators / metabolism
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Transcription Factors / chemistry
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Transcription Factors / genetics
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Transcription Factors / metabolism*
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Transcription, Genetic*
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Transcriptional Activation
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Tretinoin / pharmacology
Substances
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Adenovirus E1A Proteins
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DNA-Binding Proteins
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Nuclear Proteins
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Receptors, Retinoic Acid
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Recombinant Fusion Proteins
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STAT1 Transcription Factor
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STAT1 protein, human
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Trans-Activators
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Transcription Factors
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Tretinoin
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CREB-Binding Protein
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CREBBP protein, human
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Histone Acetyltransferases
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NCOA1 protein, human
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NCOA3 protein, human
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Nuclear Receptor Coactivator 1
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Nuclear Receptor Coactivator 3