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J Biol Chem, Vol. 273, Issue 15, 8814-8819, April 10, 1998
From the Department of Molecular Medicine, Karolinska Institute,
Karolinska Hospital, S-171 76 Stockholm, Sweden; the
Inhibition of
Na+,K+-ATPase activity by dopamine is an
important mechanism by which renal tubules modulate urine sodium
excretion during a high salt diet. However, the molecular mechanisms of this regulation are not clearly understood. Inhibition of
Na+,K+-ATPase activity in response to dopamine
is associated with endocytosis of its
Phosphorylation of the Catalyic
-Subunit Constitutes a
Triggering Signal for Na+,K+-ATPase
Endocytosis
, Department of Pharmacological and Pharmaceutical
Sciences, College of Pharmacy, University of Houston, Houston, Texas
77204; the § Department of Medicine, University of Chicago,
Chicago, Illinois 60637, and the ¶ Division de Néphrologie,
Hôpital Cantonal Universitaire, CH-1211 Geneva 14, Switzerland
- and 
-subunits, an effect
that is protein kinase C-dependent. In this study we used
isolated proximal tubule cells and a cell line derived from opossum
kidney and demonstrate that dopamine-induced endocytosis of
Na+,K+-ATPase and inhibition of its activity
were accompanied by phosphorylation of the -subunit. Inhibition of
both the enzyme activity and its phosphorylation were blocked by the
protein kinase C inhibitor bisindolylmaleimide. The early time
dependence of these processes suggests a causal link between
phosphorylation and inhibition of enzyme activity. However, after 10 min of dopamine incubation, the -subunit was no longer
phosphorylated, whereas enzyme activity remained inhibited due to its
removal from the plasma membrane. Dephosphorylation occurred in the
late endosomal compartment. To further examine whether phosphorylation
was a prerequisite for subunit endocytosis, we used the opossum kidney
cell line transfected with the rodent -subunit cDNA. Treatment
of this cell line with dopamine resulted in phosphorylation and
endocytosis of the -subunit with a concomitant decrease in
Na+,K+-ATPase activity. In contrast, none of
these effects were observed in cells transfected with the rodent
-subunit that lacks the putative protein kinase C-phosphorylation
sites (Ser11 and Ser18). Our results support
the hypothesis that protein kinase C-dependent phosphorylation of the -subunit is essential for
Na+,K+-ATPase endocytosis and that both events
are responsible for the decreased enzyme activity in response to
dopamine.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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