Adrenergic, dopaminergic, and muscarinic receptor stimulation leads to PKA phosphorylation of Na-K-ATPase.


Autoria(s): Beguin P.; Beggah A.; Cotecchia S.; Geering K.
Data(s)

1996

Resumo

Na-K-adenosinetriphosphatase (Na-K-ATPase) is a potential target for phosphorylation by protein kinase A (PKA) and C (PKC). We have investigated whether the Na-K-ATPase alpha-subunit becomes phosphorylated at its PKA or PKC phosphorylation sites upon stimulation of G protein-coupled receptors primarily linked either to the PKA or the PKC pathway. COS-7 cells, transiently or stably expressing Bufo marinus Na-K-ATPase wild-type alpha- or mutant alpha-subunits affected in its PKA or PKC phosphorylation site, were transfected with recombinant DNA encoding beta 2- or alpha 1-adrenergic (AR), dopaminergic (D1A-R), or muscarinic cholinergic (M1-AChR) receptor subspecies. Agonist stimulation of beta 2-AR or D1A-R led to phosphorylation of the wild-type alpha-subunit, as well as the PKC mutant, but not of the PKA mutant, indicating that these receptors can phosphorylate the Na-K-ATPase via PKA activation. Surprisingly, stimulation of the alpha 1B-AR, alpha 1C-AR, and M1-AChR also increased the phosphorylation of the wild-type alpha-subunit and its PKC mutant but not of its PKA mutant. Thus the phosphorylation induced by these primarily phospholipase C-linked receptors seems mainly mediated by PKA activation. These data indicate that the Na-K-ATPase alpha-subunit can act as an ultimate target for PKA phosphorylation in a cascade starting with agonist-receptor interaction and leading finally to a phosphorylation-mediated regulation of the enzyme.

Identificador

http://serval.unil.ch/?id=serval:BIB_1ED6C06C35A9

isbn:0002-9513 (Print)

pmid:8772438

isiid:A1996TT10400014

Idioma(s)

en

Fonte

American Journal of Physiology, vol. 270, no. 1 Pt 1, pp. C131-C137

Palavras-Chave #Animals; Bufo marinus/genetics; Cell Line; Cyclic AMP-Dependent Protein Kinases/agonists; Cyclic AMP-Dependent Protein Kinases/metabolism; Dopamine Agonists/pharmacology; Epinephrine/pharmacology; Muscarinic Agonists/pharmacology; Mutation; Phosphorylation; Protein Kinase C/genetics; Protein Kinase C/metabolism; Receptors, Adrenergic/metabolism; Receptors, Dopamine/metabolism; Receptors, Muscarinic/metabolism; Sodium-Potassium-Exchanging ATPase/genetics; Sodium-Potassium-Exchanging ATPase/metabolism; Transfection
Tipo

info:eu-repo/semantics/article

article