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Am J Physiol Cell Physiol (September 1, 2004). doi:10.1152/ajpcell.00284.2004
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Submitted on June 14, 2004
Accepted on August 30, 2004

Serum and glucocorticoid regulated kinase (Sgk1) inhibits insulin dependent activation of phosphomannomutase 2 (PMM2) in transfected COS-7 cells

Miranda Menniti1, Rodolfo Iuliano1, Rosario Amato1, Rosalia Boito1, Monica Corea1, Ilaria Le Pera1, Elio Gulletta1, and Nicola Perrotti1*

1 Dipartimento di Medicina Sperimentale e Clinica "G. Salvatore", Universita' Magna Graecia di Catanzaro, Catanzaro, CZ, Italy

* To whom correspondence should be addressed. E-mail: perrotti{at}unicz.it.

Serum and glucocorticoid regulated kinase (Sgk1) is considered to be an essential convergence point for peptide and steroid regulation of ENaC mediated Na+ transport. We tried to identify molecular partners of Sgk1 by yeast two hybrid screening. Yeast two hybrid screen showed a specific interaction between Sgk1 and phosphomannomutase 2 (PMM2) an enzyme involved in the regulation of glycoprotein biosynthesis. The interaction was confirmed in intact cells by coimmunoprecipitation and colocalization detected by confocal microscopy. We were then able to demonstrate that Sgk1 phosphorylates PMM2 in an in-vitro assay. In addition we found that the enzymatic activity of PMM2 is upregulated by insulin treatment and that Sgk1 completely inhibits phosphomannomutase activity both in absence and in presence of insulin stimulation. These data provide evidence suggesting that Sgk1 may modulate insulin action on cotranslational glycosylation of glycoproteins.




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