Molecular Biology of the Cell click for CBE Life Science Education Page

Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
 QUICK SEARCH:   [advanced]


     


This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Féraille, E.
Right arrow Articles by Geering, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Féraille, E.
Right arrow Articles by Geering, K.

Vol. 11, Issue 1, 39-50, January 2000

Is Phosphorylation of the alpha 1 Subunit at Ser-16 Involved in the Control of Na,K-ATPase Activity by Phorbol Ester-activated Protein Kinase C?

Eric Féraille,*dagger Dagger Pascal Béguin,dagger § Maria-Luisa Carranza,* Sandrine Gonin,* Martine Rousselot,* Pierre-Yves Martin,* Hervé Favre,* and Käthi Geering§

 *Division de Néphrologie, Hôpital Cantonal Universitaire, CH-1211 Geneva 14, Switzerland; and  §Institut de Pharmacologie et de Toxicologie de l'Université de Lausanne, CH-1005 Lausanne, Switzerland

The alpha 1 subunit of Na,K-ATPase is phosphorylated at Ser-16 by phorbol ester-sensitive protein kinase(s) C (PKC). The role of Ser-16 phosphorylation was analyzed in COS-7 cells stably expressing wild-type or mutant (T15A/S16A and S16D-E) ouabain-resistant Bufo alpha 1 subunits. In cells incubated at 37°C, phorbol 12,13-dibutyrate (PDBu) inhibited the transport activity and decreased the cell surface expression of wild-type and mutant Na,K-pumps equally (~20-30%). This effect of PDBu was mimicked by arachidonic acid and was dependent on PKC, phospholipase A2, and cytochrome P450-dependent monooxygenase. In contrast, incubation of cells at 18°C suppressed the down-regulation of Na,K-pumps and revealed a phosphorylation-dependent stimulation of the transport activity of Na,K-ATPase. Na,K-ATPase from cells expressing alpha 1-mutants mimicking Ser-16 phosphorylation (S16D or S16E) exhibited an increase in the apparent Na affinity. This finding was confirmed by the PDBu-induced increase in Na sensitivity of the activity of Na,K-ATPase measured in permeabilized nontransfected COS-7 cells. These results illustrate the complexity of the regulation of Na,K-ATPase alpha 1 isozymes by phorbol ester-sensitive PKCs and reveal 1) a phosphorylation-independent decrease in cell surface expression and 2) a phosphorylation-dependent stimulation of the transport activity attributable to an increase in the apparent Na affinity.


dagger These authors contributed equally to this work.

Dagger Corresponding author. E-mail address: feraille{at}cmu.unige.ch.


Molecular Biology of the Cell
Vol. 11, 39-50, January 2000
Copyright © 2000 by The American Society for Cell Biology



This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
J.-Y. Lee, F. Visser, J. S. Lee, K.-H. Lee, J.-W. Soh, W.-K. Ho, J. Lytton, and S.-H. Lee
Protein Kinase C-dependent Enhancement of Activity of Rat Brain NCKX2 Heterologously Expressed in HEK293 Cells
J. Biol. Chem., December 22, 2006; 281(51): 39205 - 39216.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
O. Kotova, L. Al-Khalili, S. Talia, C. Hooke, O. V. Fedorova, A. Y. Bagrov, and A. V. Chibalin
Cardiotonic Steroids Stimulate Glycogen Synthesis in Human Skeletal Muscle Cells via a Src- and ERK1/2-dependent Mechanism
J. Biol. Chem., July 21, 2006; 281(29): 20085 - 20094.
[Abstract] [Full Text] [PDF]


Home page
J. Appl. Physiol.Home page
J. I. Sznajder, P. Factor, and D. H. Ingbar
Lung Edema Clearance: 20 Years of Progress: Invited Review: Lung edema clearance: role of Na+-K+-ATPase
J Appl Physiol, November 1, 2002; 93(5): 1860 - 1866.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
S. Gonin, G. Deschênes, F. Roger, M. Bens, P.-Y. Martin, J.-L. Carpentier, A. Vandewalle, A. Doucet, and E. Féraille
Cyclic AMP Increases Cell Surface Expression of Functional Na,K-ATPase Units in Mammalian Cortical Collecting Duct Principal Cells
Mol. Biol. Cell, February 1, 2001; 12(2): 255 - 264.
[Abstract] [Full Text]


Home page
Physiol. Rev.Home page
E. Feraille and A. Doucet
Sodium-Potassium-Adenosinetriphosphatase-Dependent Sodium Transport in the Kidney: Hormonal Control
Physiol Rev, January 1, 2001; 81(1): 345 - 418.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
A. G. Therien and R. Blostein
Mechanisms of sodium pump regulation
Am J Physiol Cell Physiol, September 1, 2000; 279(3): C541 - C566.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. S. Feschenko, E. Stevenson, and K. J. Sweadner
Interaction of Protein Kinase C and cAMP-dependent Pathways in the Phosphorylation of the Na,K-ATPase
J. Biol. Chem., October 27, 2000; 275(44): 34693 - 34700.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
X. Zhong, R. Malhotra, R. Woodruff, and G. Guidotti
Mammalian Plasma Membrane Ecto-nucleoside Triphosphate Diphosphohydrolase 1, CD39, Is Not Active Intracellularly. THE N-GLYCOSYLATION STATE OF CD39 CORRELATES WITH SURFACE ACTIVITY AND LOCALIZATION
J. Biol. Chem., October 26, 2001; 276(44): 41518 - 41525.
[Abstract] [Full Text] [PDF]


Home page
Mol. Biol. CellHome page
K. M. Ridge, L. Dada, E. Lecuona, A. M. Bertorello, A. I. Katz, D. Mochly-Rosen, and J. I. Sznajder
Dopamine-induced Exocytosis of Na,K-ATPase Is Dependent on Activation of Protein Kinase C-epsilon and -delta
Mol. Biol. Cell, April 1, 2002; 13(4): 1381 - 1389.
[Abstract] [Full Text] [PDF]




Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]