RGD Reference Report - Cytoplasmic domain of natriuretic peptide receptor-C inhibits adenylyl cyclase. Involvement of a pertussis toxin-sensitive G protein. - Rat Genome Database

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Cytoplasmic domain of natriuretic peptide receptor-C inhibits adenylyl cyclase. Involvement of a pertussis toxin-sensitive G protein.

Authors: Anand-Srivastava, MB  Sehl, PD  Lowe, DG 
Citation: Anand-Srivastava MB, etal., J Biol Chem. 1996 Aug 9;271(32):19324-9.
RGD ID: 1601497
Pubmed: PMID:8702617   (View Abstract at PubMed)

Natriuretic peptide receptor C (NPR-C) is a disulfide-linked homodimer with an approximately 440-amino acid extracellular domain and a 37-amino acid cytoplasmic domain; it functions in the internalization and degradation of bound ligand. The use of NPR-C-specific natriuretic peptide analogs has implicated this receptor in mediating the inhibition of adenylyl cyclase or activation of phospholipase C. In the present studies we have investigated the role of the cytoplasmic domain of NPR-C in signaling the inhibition of adenylyl cyclase. Polyclonal rabbit antisera were raised against a 37-amino acid synthetic peptide (R37A) corresponding to the cytoplasmic domain of NPR-C. Incubation of anti-R37A with rat heart particulate fractions blocked atrial natriuretic peptide-dependent inhibition of adenylyl cyclase. The cytoplasmic domain peptides R37A and TMC (10 residues of transmembrane domain appended on R37A) were equipotent in inhibiting adenylyl cyclase (Ki approximately 1 nM) in a GTP-dependent manner, whereas K37E (a scrambled peptide control for R37A) did not inhibit adenylyl cyclase activity. Prior incubation of membranes with pertussis toxin blocked R37A or TMC inhibition of cAMP production. Detergent solubilization of the rat heart particulate fraction destroyed natriuretic peptide inhibition of adenylyl cyclase, but TMC was able to inhibit cAMP production in a dose-dependent manner. Our results provide evidence that the 37-amino acid cytoplasmic domain of NPR-C is sufficient for signaling inhibition of adenylyl cyclase through a pertussis toxin-sensitive G protein.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
negative regulation of adenylate cyclase activity  IDA 1601497 RGD 

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
identical protein binding  IPINpr3 (Rattus norvegicus)1601497homodimerizationRGD 
peptide hormone binding  IDA 1601497 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Npr3  (natriuretic peptide receptor 3)


Additional Information