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Fibroblast growth factor (FGF)-1 mitogenic signal transduction
is mediated in part by gene products that are specifically expressed in
response to cell surface receptor binding and activation. We have used
a targeted differential display method to identify FGF-1-inducible
genes in murine NIH 3T3 fibroblasts. Here we report that one of these
genes is predicted to encode a novel serine/threonine-specific protein
kinase. This putative kinase has been named Fnk, for FGF-inducible
kinase. The deduced Fnk amino acid sequence has 49, 36, 33, 32, and 22%
overall identity to mouse serum-inducible kinase (Snk), mouse polo-like
kinase (Plk), Drosophila polo, Saccharomyces Cdc5,
and mouse Snk/Plk-akin kinase (Sak), respectively. These proteins are
all members of the polo subfamily of structurally related
serine/threonine kinases. The Plk, polo, Cdc5, and Sak kinases are
required for cell division. FGF-1 induction of Fnk mRNA expression is
first detected at 30 min after mitogen addition, reflects
transcriptional activation, and does not require de novo protein synthesis. FGF-2, platelet-derived growth factor-BB, calf
serum, or phorbol myristate acetate treatment of quiescent cells also
induces fnk gene expression. Fnk mRNA is expressed in vivo in a tissue-specific manner, with relatively high levels detected
in newborn and adult mouse skin. These results indicate that Fnk may be
a transiently ex-pressed protein kinase involved in the early signaling
events required for growth factor-stimulated cell cycle progression.
Volume 270,
Number 17,
Issue of April 28, pp. 10351-10357, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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