| Title | Phosphorylated Mr 32,000 dopamine- and cAMP-regulated phosphoprotein inhibits Na+,K(+)-ATPase activity in renal tubule cells. |
| Publication Type | Journal Article |
| Year of Publication | 1991 |
| Authors | Aperia A, Fryckstedt J, Svensson L, Hemmings HC, Nairn AC, Greengard P |
| Journal | Proc Natl Acad Sci U S A |
| Volume | 88 |
| Issue | 7 |
| Pagination | 2798-801 |
| Date Published | 1991 Apr 01 |
| ISSN | 0027-8424 |
| Keywords | Amino Acid Sequence, Animals, Dopamine, Dopamine and cAMP-Regulated Phosphoprotein 32, Kidney Medulla, Kidney Tubules, Kinetics, Loop of Henle, Models, Biological, Molecular Sequence Data, Molecular Weight, Nerve Tissue Proteins, Phosphopeptides, Phosphoproteins, Phosphorylation, Rats, Sodium-Potassium-Exchanging ATPase |
| Abstract | Dopamine inhibits Na+,K(+)-ATPase activity in several renal tubule segments and thereby regulates urinary Na+ excretion. We now show that a phosphopeptide of 31 amino acids, corresponding to residues 8-38 of the protein phosphatase inhibitor DARPP-32 (dopamine- and cAMP-regulated phosphoprotein of Mr 32,000), mimics the inhibitory action of dopamine on Na+,K(+)-ATPase activity in renal tubule cells from the ascending limb of the loop of Henle. The dephosphorylated form of the peptide is ineffective. The results indicate that dopamine acts through a protein phosphorylation pathway to regulate the activity of an ion pump. In addition, the data suggest that inhibition of protein phosphatase 1 by phophorylated DARPP-32 is a component of the mechanism by which dopamine regulates urinary Na+ excretion. |
| DOI | 10.1073/pnas.88.7.2798 |
| Alternate Journal | Proc Natl Acad Sci U S A |
| PubMed ID | 1849276 |
| PubMed Central ID | PMC51326 |
| Grant List | MH 40899 / MH / NIMH NIH HHS / United States |