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(Received for publication, February 24, 1995; and in revised form, July 3, 1995)
The non-histone chromosomal protein HMG-I(Y) participates in
repression of transcription directed by a promoter which confers
interleukin 4 (IL-4)-inducible activation in transfected B cell lines.
Metabolic labeling, phosphoamino acid analyses, and in vitro phosphorylation studies demonstrate that IL-4 induces serine
phosphorylation of HMG-I(Y) in B lymphocytes. Phosphopeptide mapping
shows that the predominant site of phosphorylation contains a casein
kinase II consensus motif. The immunosuppressive agent rapamycin has
been shown preferentially to inhibit IgE production by IL-4-treated
human B cells. It is shown here that rapamycin inhibits both activation
of the human germ line promoter by IL-4 and IL-4-inducible
phosphorylation of HMG-I(Y). These findings demonstrate a
rapamycin-sensitive pathway that transduces signals from the IL-4
receptor to nuclear factors that regulate inducible transcription. The
affinity of normal nuclear HMG-I(Y) for DNA is increased by
dephosphorylation in vitro, whereas in vitro kinase
reactions using casein kinase II decrease recombinant HMG-I(Y) binding
to DNA. These data further suggest a novel mechanism in which
phosphorylation triggered by IL-4 or other cytokines could regulate the
effects of HMG-I(Y) on gene transcription.
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