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A more recent version of this article appeared on October 3, 2003
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M304098200v1
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Papers In Press, published online ahead of print July 10, 2003
J. Biol. Chem, 10.1074/jbc.M304098200
Submitted on April 18, 2003
Revised on July 10, 2003
Accepted on July 10, 2003

ANP induces natriuretic peptide receptor-PKG interaction

Nathan Airhart, Yong-Feng Yang, Charles T. Roberts . Jr, and Michael Silberbach

Pediatrics Dept., Oregon Health and Science University, Portland, OR 97034

Corresponding Author: silberbm{at}ohsu.edu

Circulating natriuretic peptides (NPs) such as atrial natriuretic peptide (ANP) counterbalance the effects of hypertension and inhibit cardiac hypertrophy by activating cGMP-dependent protein kinase (PKG). NP binding to type I receptors (NPRA and NPRB) activates their intrinsic guanylyl cyclase activity, resulting in a rapid increase in cytosolic cGMP that subsequently activates PKG. Phosphorylation of the receptor by an unknown serine/threonine kinase is required before ligand binding can activate the cyclase. While searching for downstream PKG partners using a yeast two-hybrid screen of a human heart cDNA library, we unexpectedly found an upstream association with NPRA. PKG is itself a serine/threonine kinase capable of phosphorylating NPRA in vitro; however, regulation of NPRA by PKG has not been previously reported. Here we show that PKG is recruited to the plasma membrane following ANP treatment, an effect that can be blocked by pharmacological inhibition of PKG activation. Furthermore, PKG participates in a ligand-dependent, gain-of-function loop that significantly increases the intrinsic cyclase activity of the receptor. PKG translocation is ANP-dependent, but not NO-dependent. Our results suggest that anchoring of PKG to NPRA is a key event after ligand binding that determines distal effects. As such, the NPRA-PKG association may represent a novel mechanism for compartmentation of cGMP-mediated signaling and regulation of receptor sensitivity.


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