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Physiology 21: 326-335, 2006; doi:10.1152/physiol.00015.2006
1548-9213/06 $8.00
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Physiology, Vol. 21, No. 5, 326-335, October 2006
© 2006 Int. Union Physiol. Sci./Am. Physiol. Soc.

REVIEW

WNK Protein Kinases Modulate Cellular Cl– Flux by Altering the Phosphorylation State of the Na-K-Cl and K-Cl Cotransporters

Kristopher T. Kahle1,2, Jesse Rinehart1, Aaron Ring1, Ignacio Gimenez3, Gerardo Gamba4, Steven C. Hebert2 and Richard P. Lifton1

1 Howard Hughes Medical Institute, and Departments of Genetics, Medicine, and Molecular Biophysics and Biochemistry, and
2 Cellular and Molecular Physiology, Yale University School of Medicine, New Haven, Connecticut;
3 Department of Pharmacology and Physiology, School of Medicine, University of Zaragoza, Zaragoza, Spain; and
4 Molecular Physiology Unit, Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México and Instituto Nacional de Ciencias Médicas y Nutrición Salvador Zubirán, Tlalpan, Mexico City, Mexico

Precise control of cellular Cl– transport is necessary for many fundamental physiological processes. For example, the intracellular concentration of Cl–, fine-tuned through the coordinated action of cellular Cl– influx and efflux mechanisms, determines whether a neuron’s response to GABA is excitatory or inhibitory. In epithelia, synchrony between apical and basolateral Cl– flux, and transcellular and paracellular Cl– transport, is necessary for efficient transepithelial Cl– reabsorption or secretion. In cells throughout the body, coordination of Cl– entry and exit mechanisms help defend against changes in cell volume. The Na-K-Cl and K-Cl cotransporters of the SLC12 gene family are important molecular determinants of Cl– entry and exit, respectively, in these systems. The WNK serine-threonine kinase family, members of which are mutated in an inherited form of human hypertension, are components of a signaling pathway that coordinates Cl– influx and efflux through SLC12 cotransporters to dynamically regulate intracellular Cl– activity.




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