cGMP Signaling through cAMP- and cGMP-Dependent Protein Kinases
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Cited by (88)
Fine tuning by protein kinases of Ca<inf>V</inf>1.2 channel current in rat tail artery myocytes
2020, Biochemical PharmacologyCitation Excerpt :Furthermore, the use of such agents has inherent limitations [3] due, for example, to the cross-talk between PKG and PKA. These proteins, in fact, despite exhibiting a 50- to 200-fold higher selectivity for cGMP and cAMP, can also be activated by physiological concentrations of cAMP and cGMP, respectively [19,25,8,14]; this may obscure the real upstream signal responsible for the final, biological effect. Furthermore, the existence of subcellular micro-domains and compartmentation of proteins supporting these pathways may further confound this scenario [58].
Epac in cardiac calcium signaling
2013, Journal of Molecular and Cellular CardiologyCitation Excerpt :cAMP is one of the most important second messengers in the heart, regulating many physiological processes, such as cardiac contractility, relaxation, and automaticity. Although protein kinase A (PKA) is generally recognized as the primary effector of cAMP signaling [2], other effectors are known to transduce cyclic nucleotide-encoded information. They encompass a class of cyclic nucleotide gated (CNG) cation channels and phosphodiesterases (PDEs) [3,4].
Myristoylation of cGMP-dependent protein kinase dictates isoform specificity for serotonin transporter regulation
2011, Journal of Biological ChemistryCitation Excerpt :Myristoylation and consequent membrane targeting of PKGII are required for its ability to phosphorylate several proteins including the cystic fibrosis transmembrane conductance regulator Cl− channel (20). Structurally, PKG is a homodimer consisting of a typical protein kinase domain at the C terminus, a regulatory domain that binds cGMP, and an N-terminal heptad leucine/isoleucine repeat responsible for dimerization and interaction with substrates (21–23). Both PKGI and PKGII are predominantly present in most brain regions and play critical roles in the regulation of brain function (24–26).
Phosphorylation and activation of a transducible recombinant form of human HSP20 in Escherichia coli
2007, Protein Expression and PurificationCyclic nucleotide signaling in cavernous smooth muscle
2005, Journal of Sexual MedicineCitation Excerpt :An earlier study showed that PKG was activated by cAMP in rat AOSMC, leading to a reduction in intracellular Ca2+[85]. Overexpression of NOS, which leads to increased levels of NO and cGMP, was also shown to result in cross‐activation of PKA [86]. Whether cross‐activation of PKA and PKG plays physiological roles has been questioned in a study with PKG‐I‐deficient mice.
Regulation of nitric oxide and soluble guanylyl cyclase
2004, Brain Research Bulletin