Identification and Characterization of the Major Phosphorylation Sites of the B-type Natriuretic Peptide Receptor
Key result
Elimination of all major phosphorylation sites in the kinase homology domain of NPR-B resulted in a completely dephosphorylated receptor with >90% decreased CNP-dependent cyclase activity.
Population
Human 293 cells expressing Natriuretic peptide receptor-B (NPR-B)
Comparison
Mutagenesis of specific residues to alanine vs Wild-type/unmutated NPR-B
Design
Preclinical
Authors
Discussion
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Member takes
Implication
NPR-B phosphorylation sites mapped; extends molecular understanding of CNP desensitization but leaves open clinical translation to vasorelaxation.
Structured PICO
P
Population
Human 293 cells expressing Natriuretic peptide receptor-B (NPR-B)
I
Intervention
Mutagenesis of specific residues (Ser-513, Thr-516, Ser-518, Ser-523, Ser-526, Gly-521, and Ser-522) to alanine
C
Comparator
Wild-type/unmutated NPR-B
O
Outcome
Receptor phosphorylation state and CNP-dependent guanylyl cyclase activitysurrogate
Identification of specific phosphorylation sites on NPR-B demonstrates that phosphorylation of the kinase homology domain is critical for its CNP-dependent guanylyl cyclase activity.
Cite This Study
Potter et al. (1998) studied this question. Mutagenesis of NPR-B phosphorylation sites vs. Wild-type NPR-B was evaluated on CNP-dependent guanylyl cyclase activity and receptor phosphorylation state. Elimination of all major phosphorylation sites in the kinase homology domain of NPR-B resulted in a completely dephosphorylated receptor with >90% decreased CNP-dependent cyclase activity.