Abstract
To achieve maximal transcriptional activity in response to gp130 cytokines, Serine-727 (Ser-727) of Stat3 is phosphorylated. Ser-727 resides in the LPMSP motif, the only conserved sequence among the transcription activation domains of several STATs. We show here that in addition to Ser-727, other residues in this LPMSP motif are also required for Stat3 activity in response to cytokine signaling through regulation of Ser-727 phosphorylation and recruitment of the transcription co-activator CBP/p300 to the promoters of Stat3-target genes for transcription activation. Hence, we have demonstrated a critical role for the whole conserved LPMSP motif in JAK-STAT signaling.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Motifs
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Amino Acid Substitution
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Animals
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Base Sequence
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Cells, Cultured
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Conserved Sequence
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DNA Primers / genetics
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Interleukin-6 / pharmacology*
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Mice
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Oncostatin M / pharmacology*
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Phosphorylation
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Proline / chemistry
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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STAT3 Transcription Factor / chemistry
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STAT3 Transcription Factor / deficiency
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STAT3 Transcription Factor / genetics
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STAT3 Transcription Factor / metabolism*
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Serine / chemistry
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Signal Transduction / drug effects
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Transcriptional Activation
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Transfection
Substances
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DNA Primers
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Interleukin-6
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Recombinant Proteins
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STAT3 Transcription Factor
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Stat3 protein, mouse
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Oncostatin M
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Serine
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Proline