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Am J Physiol Cell Physiol 292: C1971-C1981, 2007. First published January 3, 2007; doi:10.1152/ajpcell.00399.2006
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CELLULAR METABOLISM

Subcellular location of serum- and glucocorticoid-induced kinase-1 in renal and mammary epithelial cells

Emily Cordas, Anikó Náray-Fejes-Tóth, and Géza Fejes-Tóth

Department of Physiology, Dartmouth Medical School, Lebanon, New Hampshire

Submitted 21 July 2006 ; accepted in final form 28 December 2006

Serum- and glucocorticoid-induced kinase-1 (SGK1) is involved in aldosterone-induced Na+ reabsorption by increasing epithelial Na+ channel (ENaC) activity in cortical collecting duct (CCD) cells, but its exact mechanisms of action are unknown. Although several potential targets such as Nedd4-2 have been described in expression systems, endogenous substrates mediating SGK1's physiological effects remain to be identified. In addition, subcellular localization studies of SGK1 have provided controversial results. We determined the subcellular location of SGK1 using SGK1-autofluorescent protein (AFP) fusion proteins. Rabbit CCD (RCCT-28A) cells were transiently transfected with a construct encoding for SGK1-AFP and were stained or cotransfected with markers for various subcellular compartments. In live cells, transiently expressed SGK1-AFP clearly colocalized with the mitochondrial marker rhodamine 123. Similarly, SGK1-AFP colocalized with the mitochondrial marker MitoTracker when stably expressed using a retroviral system in either RCCT-28A cells or the mammary epithelial cell line MCF10A. To determine which region of SGK1 is responsible for this subcellular localization, we generated RCCT-28A cell lines stably expressing SGK1 mutants. The results indicate that the NH2-terminal 60-amino acid region of SGK1 is necessary and sufficient for its subcellular localization. Localization of SGK1 to the mitochondria raises the possibility that SGK1 may play a role in regulating energy metabolism.

mitochondria; localization


Address for reprint requests and other correspondence: G. Fejes-Tóth, Dept. of Physiology, Dartmouth Medical School, 1 Medical Center Dr., Lebanon, NH 03756 (e-mail: geza.fejes-toth{at}dartmouth.edu)






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