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MBC in Press, published online ahead of print September 5, 2007
Mol. Biol. Cell 10.1091/mbc.E06-08-0711

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Submitted on August 15, 2006
Revised on July 31, 2007
Accepted on August 28, 2007

Arrestins and Spinophilin Competitively Regulate Na+,K+-ATPase Trafficking through Association with a Large Cytoplasmic Loop of the Na+,K+-ATPase

Tohru Kimura,* Patrick B. Allen,{dagger} Angus C. Nairn,{dagger} and Michael J. Caplan*

Departments of *Cellular and Molecular Physiology and {dagger}Psychiatry, Yale University School of Medicine, New Haven, CT 06520-8026

Monitoring Editor: J. Silvio Gutkind

The activity and trafficking of the Na+,K+-ATPase are regulated by several hormones, including dopamine, vasopression and adrenergic hormones through the action of G–protein-coupled receptors (GPCRs). Arrestins, GPCR kinases (GRKs), 14–3-3 proteins, and spinophilin interact with GPCRs and modulate the duration and magnitude of receptor signaling. We have found that arrestin 2 and 3, GRK2 and 3, 14–3-3 {varepsilon} and spinophilin directly associate with the Na+,K+-ATPase and that the associations with arrestins, GRKs or 14–3-3 {varepsilon} are blocked in the presence of spinophilin. In COS cells that overexpressed arrestin, the Na+,K+-ATPase was redistributed to intracellular compartments. This effect was not seen in mock-transfected cells or in cells expressing spinophilin. Furthermore, expression of spinophilin appeared to slow, whereas overexpression of {beta}-arrestins accelerated internalization of the Na+,K+-ATPase endocytosis. We also find that GRKs phosphorylate the Na+,K+-ATPase in vitro on its large cytoplasmic loop. Taken together, it appears that association with arrestins, GRKs, 14–3-3 {varepsilon} and spinophilin may be important modulators of Na+,K+-ATPase trafficking.

Address correspondence to: Michael J. Caplan (michael.caplan{at}yale.edu)




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