 | Na,K-ATPase AND RELATED CATION PUMPS: Structure, Function, and Regulatory Mechanisms
Copyright © 2003 by the New York Academy of Sciences
description
Annals of the New York Academy of Sciences 986:587-594 (2003)
© 2003 New York Academy of Sciences
Isoform-Specific Regulation of Na+,K+-ATPase Endocytosis and Recruitment to the Plasma Membrane
VERA LUCAS TEIXEIRAa,
ADRIAN I. KATZb,
CARLOS H. PEDEMONTEc AND
ALEJANDRO M. BERTORELLOa
aDepartment of Medicine, Atherosclerosis Research Unit, Karolinska Institutet, Karolinska Hospital, 171 76 Stockholm, Sweden
bDepartment of Medicine, University of Chicago, Chicago, Illinois 60637
cCollege of Pharmacy, University of Houston, Houston, Texas 77204
Address for correspondence: Alejandro M. Bertorello, Department of Medicine, King Gustaf V Research Institute, M1, Karolinska Hospital, 171 76 Stockholm, Sweden. Voice: +46-8-5177-3224; fax: +46-8-31-12-98.
alejandro.bertorello{at}molmed.ki.se
Ann. N.Y. Acad. Sci. 986: 587-594 (2003).
The Na +,K +-ATPase traffics between the plasma membrane and intracellular compartments in response to acute changes in membrane receptor activation. These effects are accomplished by a time-dependent interaction of the Na +,K +-ATPase  -subunit with specific intracellular signaling molecules either at the plasma membrane (endocytosis) or at the endosome's membranes (recruitment). Most of these studies have been performed in rat renal epithelial cells in which only the 1 isoenzyme is present. Studies in neurons from the neostriatum in which all three -subunit isoforms are present indicate that neurotransmitter-dependent regulation of Na +,K +-ATPase activity displays isoform specificity and also suggest a more complex organization of the intracellular signaling networks controlling Na +,K +-ATPase traffic in mammalian cells.
Key Words: Na+,K+-ATPase isoforms • endocytosis • catecholamines • neostriatal neurons • protein phosphorylation
This article has been cited by other articles:
|
|
|
|
 
T. Feldmann, V. Glukmann, E. Medvenev, U. Shpolansky, D. Galili, D. Lichtstein, and H. Rosen
Role of endosomal Na+-K+-ATPase and cardiac steroids in the regulation of endocytosis
Am J Physiol Cell Physiol,
September 1, 2007;
293(3):
C885 - C896.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
E. Lecuona, L. A. Dada, H. Sun, M. L. Butti, G. Zhou, T.-L. Chew, and J. I. Sznajder
Na,K-ATPase {alpha}1-subunit dephosphorylation by protein phosphatase 2A is necessary for its recruitment to the plasma membrane
FASEB J,
December 1, 2006;
20(14):
2618 - 2620.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
K Wagoner, G Sanchez, A-N Nguyen, G C Enders, and G Blanco
Different expression and activity of the {alpha}1 and {alpha}4 isoforms of the Na,K-ATPase during rat male germ cell ontogeny
Reproduction,
November 1, 2005;
130(5):
627 - 641.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
|
|
|
R. Efendiev, Z. Chen, R. T. Krmar, S. Uhles, A. I. Katz, C. H. Pedemonte, and A. M. Bertorello
The 14-3-3 Protein Translates the NA+,K+-ATPase {alpha}1-Subunit Phosphorylation Signal into Binding and Activation of Phosphoinositide 3-Kinase during Endocytosis
J. Biol. Chem.,
April 22, 2005;
280(16):
16272 - 16277.
[Abstract]
[Full Text]
[PDF]
|
|
|
|
