Dopamine-induced Endocytosis of Na+,K+-ATPase Is Initiated by Phosphorylation of Ser-18 in the Rat α Subunit and Is Responsible for the Decreased Activity in Epithelial Cells

Chibalin, Alexander V.; Ogimoto, Goichi; Pedemonte, Carlos H.; Pressley, Thomas A.; Katz, Adrian I.; Féraille, Eric; Berggren, Per Olof; Bertorello, Alejandro M.

doi:10.1074/jbc.274.4.1920

Cited by 195 publications

(242 citation statements)

References 41 publications

Supporting

Mentioning

227

Contrasting

Unclassified

Order By: Relevance

“…Catecholamines, especially dopamine, are involved in the regulation of Na + excretion during salt load or deprivation (Aperia 2000). Dopamine stimulates the phosphorylation of Na + /K + ATPase α-subunits in kidney tubules (Chibalin et al 1999) and activates PI3 kinases, the products of which, such as phosphatidyl-inositol-3-phosphate, are essential for the clathrin-dependent endocytosis of the Na + /K + ATPase by mediating the interaction of the adaptor protein adaptin (AP2) with a tyrosine motif in the Na + /K + ATPase α-subunit (Ogimoto et al 2000;Done et al 2002).…”

Section: Polymorphisms In Adducin Genesmentioning

confidence: 99%

Genetics of arterial hypertension and hypotension

Rosskopf

Schürks

Rimmbach

et al. 2007

Naunyn-Schmied Arch Pharmacol

View full text Add to dashboard Cite

Human hypertension affects affects more than 20% of the adult population in industrialized countries, and it is implicated in millions of deaths worldwide each year from stroke, heart failure and ischemic heart disease. Available evidence suggests a major genetic impact on blood pressure regulation. Studies in monogenic hypertension revealed that renal salt and volume regulation systems are predominantly involved in the genesis of these disorders. Mutations here affect the synthesis of mineralocorticoids, the function of the mineralocorticoid receptor, epithelial sodium channels and their regulation by a new class of kinases, termed WNK kinases. It has been learned from monogenic hypotension that almost all ion transporters involved in the renal uptake of Na + have a major impact on blood pressure regulation. For essential hypertension as a complex disease, many candidate genes have been analysed. These include components of the reninangiotensin-aldosterone system, adducin, β-adrenoceptors, G protein subunits, regulators of G protein signalling (RGS) proteins, Rho kinases and G protein receptor kinases. At present, the individual impact of common polymorphisms in these genes on the observed blood pressure variation, on risk for stroke and as predictors of antihypertensive responses remains small and clinically irrelevant. Nevertheless, these studies have greatly augmented our knowledge on the regulation of renal functions, cellular signal transduction and the integration of both. Together, this provides the basis for the identification of novel drug targets and, hopefully, innovative antihypertensive drugs.

show abstract

Section: Polymorphisms In Adducin Genesmentioning

confidence: 99%

Genetics of arterial hypertension and hypotension

Rosskopf

Schürks

Rimmbach

et al. 2007

Naunyn-Schmied Arch Pharmacol

View full text Add to dashboard Cite

show abstract

“…The expression vector pCMV containing the rodent Na ϩ -pump ␣1-subunit cDNA was obtained from PharMingen. Mutants of ␣1 were prepared, as previously described (12)(13)(14)(15), from a plasmid containing the wild type ␣-subunit sequence and complementary oligonucleotides containing the desired change. Briefly, annealed plasmid and oligonucleotides were subjected to PCR amplification with Pfu polymerase, followed by restriction of the original wild type template with DpnI.…”

Section: Methodsmentioning

confidence: 99%

Agonist-dependent Regulation of Renal Na+, K+-ATPase Activity Is Modulated by Intracellular Sodium Concentration

Efendiev

Bertorello

Zandomeni

et al. 2002

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

We tested the hypothesis that the level of intracellular sodium modulates the hormonal regulation of the Na ؉ ,K ؉ -ATPase activity in proximal tubule cells. By using digital imaging fluorescence microscopy of a sodium-sensitive dye, we determined that the sodium ionophore monensin induced a dose-specific increase of intracellular sodium. A correspondence between the elevation of intracellular sodium and the level of dopamine-induced inhibition of Na ؉ ,K ؉ -ATPase activity was determined. At basal intracellular sodium concentration, stimulation of cellular protein kinase C by phorbol 12-myristate 13-acetate (PMA) promoted a significant increase in Na ؉ ,K ؉ -ATPase activity; however, this activation was gradually reduced as the concentration of intracellular sodium was increased to become a significant inhibition at concentrations of intracellular sodium higher than 16 mM. Under these conditions, PMA and dopamine share the same signaling pathway to inhibit the Na ؉ ,K ؉ -ATPase. The effects of PMA and dopamine on the Na ؉ ,K ؉ -ATPase activity and the modulation of these effects by different intracellular sodium concentrations were not modified when extracellular and intracellular calcium were almost eliminated. These results suggest that the level of intracellular sodium modulates whether hormones stimulate, inhibit, or have no effect on the Na ؉ ,K ؉ -ATPase activity leading to a tight control of sodium reabsorption.

show abstract

“…At the cellular level, inhibition of Na ϩ ,K ϩ -ATPase activity is mediated by removal of active molecules from the plasma membrane and their transport into early and late endosomes via a clathrin-coated vesicle-dependent mechanism (9 -11). PKC--dependent phosphorylation of Na ϩ ,K ϩ -ATPase ␣-subunit constitutes a triggering signal for endocytosis (11,12) by facilitating the activation of phosphatidylinositol 3-kinase (PI 3-kinase) (13,14). This effect involves the interaction of PI 3-kinase (p85␣-SH3 domain) with a proline-rich domain (PRD) located upstream of the phosphorylated residue (Ser 18 ) within the Na ϩ ,K ϩ -ATPase ␣-subunit (14).…”

mentioning

confidence: 99%