Background
Although the cGMP-dependent protein kinase type I (cGKI) is an important mediator of cGMP signaling in many cells and tissues, its’ in vivo-biochemistry is not well understood. It has been shown that the purified enzyme can autophosphorylate multiple sites in its N-terminal region in the presence of ATP and cyclic nucleotides (cGMP and/or cAMP). N-terminal autophosphorylation might be involved in the activation of the kinase by cGMP in vitro, but it is not clear whether or not this also happens in intact cells [1].