cGMP-dependent phosphorylation and degradation of myristoylated alanine-rich C-kinase substrate.
In the mammalian brain, nitric oxide (NO) has been implicated in neuronal signal transmissions. NO stimulates guanylate cyclase to increase intracellular cGMP, which in turn activates cGMP-dependent protein kinases (PKG), but the targets of PKG in the brain have not fully been understood. In this study, we examined cGMP-dependent phosphorylation of proteins in rat brain and found that one of the possible substrates was myristoylated alanine-rich C-kinase substrate (MARCKS), an actin-binding membrane-associated protein that regulates cell adhesion. In addition, possible degradation products of MARCKS were observed after transfection of PKG or stimulation with 8pCPT-cGMP. Western blot analysis showed that the MARCKS protein levels were decreased when the cells were stimulated with 8pCPT-cGMP. These results suggest that MARCKS is a target of PKG, and PKG-dependent phosphorylation of MARCKS results in its degradation to reduce its protein levels in the cells.[1]References
- cGMP-dependent phosphorylation and degradation of myristoylated alanine-rich C-kinase substrate. Matsubara, T., Okumura, N., Okumura, A., Nagai, K. Biochem. Biophys. Res. Commun. (2005) [Pubmed]
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