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Am J Physiol Cell Physiol 284: C1255-C1261, 2003; doi:10.1152/ajpcell.00520.2002
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Vol. 284, Issue 5, C1255-C1261, May 2003

Identification of the G protein-activating sequence of the single-transmembrane natriuretic peptide receptor C (NPR-C)

Huiping Zhou and Karnam S. Murthy

Departments of Physiology and Medicine, Medical College of Virginia Campus, Virginia Commonwealth University, Richmond, Virginia 23298

Rat natriuretic peptide clearance receptor (NPR-C) contains four sequences capable of inhibiting adenylyl cyclase. We have undertaken mutational and deletion studies on the intracellular domain of rat NPR-C to determine which of these sequences is functionally relevant. Nine mutant receptors were constructed by deletion of 11 or 28 COOH-terminal residues or by site-directed mutagenesis of basic residues in a 17-amino acid sequence, R469RNHQEESNIGKHRELR485, corresponding to the main active peptide. Substitution of arginine residues (R469R470) flanking the NH2 terminus abolished Gi1 and Gi2 and PLC-beta activities and inhibition of adenylyl cyclase. Substitution of one or two basic residues (H481 and/or R482 or R485) in the COOH-terminal motif (H481RELR485) greatly decreased or abolished G protein and PLC-beta activities and inhibition of adenylyl cyclase. This implies that sequences NH2-terminal to the motif or COOH-terminal to R470 could not sustain receptor activity in situ, although they exhibited activity when used as synthetic peptides. Deletion of the 11 COOH-terminal residues (E486 to A496) suggested an autoinhibitory function for this sequence. We conclude that the 17-amino acid sequence (R469 to R485) in the middle region of the intracellular domain of NPR-C is both necessary and sufficient for activation of G proteins and effector enzymes.

phospholipase C-beta ; adenylyl cyclase; G protein-coupled receptors; natriuretic peptide clearance receptor


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