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Department of Veterinary Pathobiology, University of Missouri, Columbia, MO 65211
Serum amyloid A-activating factor-1 (SAF-1) is a zinc finger
transcription factor that is activated by many mediators of
inflammation including IL-1, IL-6, and bacterial LPS. However, the
mechanism of activation is not fully understood. To identify possible
activation partners for SAF-1, we used a yeast two-hybrid system that
detected interaction between the catalytic subunit of cyclic
AMP-dependent protein kinase (PKA-C
) and SAF-1. Immunofluorescence
and combined immunoprecipitation-Western blot analyses revealed
colocalization and interaction between SAF-1 and PKA-C. In vivo
evidence of SAF-1 and PKA-C interaction was further revealed by
coimmunoprecipitation of these two proteins in cAMP-activated liver
cells. We further show that SAF-1 is phosphorylated in vitro by
PKA-C and that addition of cAMP markedly induces in vivo
phosphorylation of SAF-1 and transcription of SAF-regulated reporter
genes. These results showed that SAF1-PKA-C interaction is involved
in functional activation of SAF-1.
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