Article
Protein kinase G phosphorylates soluble guanylyl cyclase on serine 64 and inhibits its activity.
Arteriosclerosis, thrombosis, and vascular biology - 1 Oct 2008
Zhou Zongmin, Sayed Nazish, Pyriochou Anastasia, Roussos Charis, Fulton David, Beuve Annie, Papapetropoulos Andreas
Abstract excerpt
OBJECTIVE: Binding of nitric oxide (NO) to soluble guanylyl cyclase (sGC) leads to increased cGMP synthesis that activates cGMP-dependent protein kinase (PKG). Herein, we tested whether sGC activity is regulated by PKG. METHODS AND RESULTS: Overexpression of a constitutively active form of PKG (DeltaPKG) stimulated (32)P incorporation into the alpha1 subunit. Serine to alanine mutation of putative sites revealed...
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