TY - JOUR
T1 - Phosphorylation of soluble guanylyl cyclase by the cyclic AMP-dependent protein kinase (PKA)
AU - Pyriochou, Anastasia
AU - Tsarbopoulos, Antonis
AU - Papapetropoulos, Andreas
PY - 2006
Y1 - 2006
N2 - Soluble guanylyl cyclase (sGC) has been shown to be regulated by transcriptional, post-transcriptional and post-translational mechanisms. Post-translationally sGC activity and subcellular localization is regulated by both phosphorylation and protein-protein interactions. The aim of the present study was to determine whether sGC is a cAMP-dependent protein kinase (PKA) substrate. We provide evidence that both of and β1 sGC can be phosphorylated by PKA.
AB - Soluble guanylyl cyclase (sGC) has been shown to be regulated by transcriptional, post-transcriptional and post-translational mechanisms. Post-translationally sGC activity and subcellular localization is regulated by both phosphorylation and protein-protein interactions. The aim of the present study was to determine whether sGC is a cAMP-dependent protein kinase (PKA) substrate. We provide evidence that both of and β1 sGC can be phosphorylated by PKA.
KW - Phosphorylation
KW - Soluble guanylyl cyclase
KW - cAMP-dependent protein kinase
KW - cGMP
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M3 - Article
AN - SCOPUS:33744462883
SN - 1011-6583
VL - 20
SP - 311
EP - 313
JO - Review of Clinical Pharmacology and Pharmacokinetics, International Edition
JF - Review of Clinical Pharmacology and Pharmacokinetics, International Edition
IS - 2
ER -