Microinjection of the Catalytic Subunit of cAMP-dependent Protein Kinase Induces Expression of the c-fos Gene

  1. K.T. Riabowol*,
  2. M.Z. Gilman*, and
  3. J.R. Feramisco
  1. *Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724; Cancer Center, University of California-San Diego, California 92103

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Excerpt

Changes in the concentration of cAMP have been shown to regulate cell shape (Porter et al. 1974) and metabolism (Schacter et al. 1984) and have been implicated in the inhibition of cell growth (Otten et al. 1972), although it is now believed that a sustained increase in the cellular level of cAMP constitutes a growth-promoting signal in mammalian (Rozengurt 1986) and yeast (Matsumoto et al. 1985) cells. In Escherichia coli, the expression of genes encoding enzymes involved in sugar catabolism is activated following binding of cAMP to a catabolite gene-activator protein (cap) and subsequent binding of the complex to specific DNA sequences of cAMP-regulated genes (de Crombrugghe et al. 1984). In contrast, the major way by which cAMP exerts cellular effects in eukaryotes is thought to be through the cAMP-dependent protein kinase (A-kinase) (Beavo et al. 1974). The holoenzyme of A-kinase exists as an enzymatically inactive tetramer, composed of two...

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