Abstract
PIAS3, a member of the protein inhibitor of activated STAT family, was found to interact in vivo and in vitro with TIF2, a previously described coactivator for nuclear receptors. The interaction is mediated by two distinct non-contiguous regions of TIF2. We found that TIF2-PIAS3 interaction occurs through a unique domain of PIAS3, very rich in acidic residues and conserved throughout the PIAS family. PIAS3 modulates the ability of TIF2 to mediate ligand-enhanced transcription activation positively or negatively, for different steroid receptors. Taken together, our results indicate a potential role of PIAS3 as transcriptional modulator of TIF2-mediated signalling.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Androgens / pharmacology
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Animals
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Base Sequence
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Binding Sites
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COS Cells
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Carrier Proteins / genetics
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Carrier Proteins / physiology*
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Chlorocebus aethiops
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Cloning, Molecular
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DNA Primers
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Embryo, Mammalian
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Glucocorticoids / pharmacology
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Intracellular Signaling Peptides and Proteins*
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Methionine / metabolism
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Mice
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Mutagenesis
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Nuclear Proteins / metabolism
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Nuclear Receptor Coactivator 2
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Protein Inhibitors of Activated STAT
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Receptors, Progesterone / physiology
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Recombination, Genetic
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Saccharomyces cerevisiae / genetics
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Sequence Deletion
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Signal Transduction / physiology*
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Transcription Factors / genetics*
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Transcription Factors / metabolism*
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Transcriptional Activation / drug effects
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Transcriptional Activation / physiology*
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Transfection
Substances
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Androgens
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Carrier Proteins
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DNA Primers
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Glucocorticoids
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Intracellular Signaling Peptides and Proteins
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Ncoa2 protein, mouse
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Nuclear Proteins
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Nuclear Receptor Coactivator 2
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Pias3 protein, mouse
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Protein Inhibitors of Activated STAT
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Receptors, Progesterone
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Transcription Factors
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Methionine