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J Biol Chem, Vol. 274, Issue 4, 1920-1927, January 22, 1999
From the Department of Molecular Medicine, Karolinska Institutet,
The Rolf Luft Center for Diabetes Research, Karolinska Hospital, S-171
76 Stockholm, Sweden, the Dopamine inhibits
Na+,K+-ATPase activity in renal tubule
cells. This inhibition is associated with phosphorylation and
internalization of the We conclude that dopamine-induced inhibition of
Na+,K+-ATPase activity in rat renal tubule
cells requires endocytosis of the
Dopamine-induced Endocytosis of
Na+,K+-ATPase Is Initiated by Phosphorylation
of Ser-18 in the Rat
Subunit and Is Responsible for the
Decreased Activity in Epithelial Cells
,
, Department of Pharmacological
and Pharmaceutical Sciences, College of Pharmacy, University of
Houston, Houston, Texas 77204, the § Department of
Physiology, Texas Tech University, Lubbock, Texas 79430, the
¶ Department of Medicine, University of Chicago, Chicago, Illinois
60637, and the Division de Néphrologie, Hôpital
Cantonal Universitaire, CH-1211 Geneva 14, Switzerland
subunit, both events being protein kinase
C-dependent. Studies of purified preparations, fusion
proteins with site-directed mutagenesis, and heterologous expression
systems have identified two major protein kinase C phosphorylation
residues (Ser-11 and Ser-18) in the rat 1 subunit
isoform. To identify the phosphorylation site(s) that mediates
endocytosis of the subunit in response to dopamine, we have performed
site-directed mutagenesis of these residues in the rat 1
subunit and expressed the mutated forms in a renal epithelial cell
line. Dopamine inhibited Na+,K+-ATPase activity
and increased subunit phosphorylation and
clathrin-dependent endocytosis into endosomes in cells
expressing the wild type 1 subunit or the S11A
1 mutant, and both effects were blocked by protein
kinase C inhibition. In contrast, dopamine did not elicit any of these
effects in cells expressing the S18A 1 mutant. While Ser-18 phosphorylation is necessary for endocytosis, it does not affect
per se the enzymatic activity: preventing endocytosis with wortmannin or LY294009 blocked the inhibitory effect of dopamine on
Na+,K+-ATPase activity, although it did not
alter the increased subunit phosphorylation induced by this agonist.
subunit into defined
intracellular compartments and that phosphorylation of Ser-18 is
essential for this process.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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