Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Subscribe

Sci. STKE, 13 November 2001
Vol. 2001, Issue 108, p. re17
[DOI: 10.1126/stke.2001.108.re17]

REVIEWS

Regulation and Physiological Roles of Serum- and Glucocorticoid-Induced Protein Kinase Isoforms

Florian Lang1 and Philip Cohen2

1Department of Physiology, University of Tubingen, Germany.
2Medical Research Council Protein Phosphorylation Unit, School of Life Sciences, University of Dundee, Dundee, Scotland, DD1 4HN, United Kingdom.

Gloss: The covalent attachment of phosphate to proteins (phosphorylation), catalyzed by enzymes known as protein kinases, and the removal of phosphate from proteins (dephosphorylation), catalyzed by protein phosphatases, regulate most aspects of cell life. Phosphorylation or dephosphorylation alters the conformation of a protein and can change its ability to function in almost every conceivable way. For example, it cannot only switch activity on or off, but alter the rate at which a protein is degraded or its ability to move from one subcellular compartment to another. There are about 500 protein kinases and 150 protein phosphatases encoded by the human genome, and discovering their biological roles is one of the major tasks of the postgenomic era. This article reviews our current knowledge about one of the protein kinase subfamilies, termed serum- and glucocorticoid-induced protein kinases because the first member (SGK1) was identified as a gene that is rapidly transcribed into mRNA when cells are stimulated by serum or glucocorticoid hormones. However, we now know that the SGK1 gene is transcribed in response to a great variety of extracellular signals. Moreover, the SGK1 enzyme is itself activated by phosphorylation in response to different extracellular signals that act via the formation of a lipid mediator called phosphatidylinositol-3,4,5-trisphosphate (PIP3). Evidence is accumulating that SGK1 plays important roles in activating certain potassium, sodium, and chloride channels, suggesting an involvement in the regulation of processes such as cell survival, the functioning of the brain, and the excretion of sodium by the kidney. For the last mentioned reason, sustained high levels of SGK1 protein and activity may contribute to diseases and conditions, such as hypertension and long-term damage to the kidney in type II diabetes. This raises the possibility that drugs that inhibit SGK1 specifically may have therapeutic potential for the treatment of several diseases.

Contact authors: E-mail:p.cohen{at}dundee.ac.uk, florian.lang{at}uni-tuebingen.de

Citation: F. Lang, P. Cohen, Regulation and Physiological Roles of Serum- and Glucocorticoid-Induced Protein Kinase Isoforms. Sci. STKE 2001, re17 (2001).


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Coxsackievirus B3 modulates cardiac ion channels.
K. Steinke, F. Sachse, N. Ettischer, N. Strutz-Seebohm, U. Henrion, M. Rohrbeck, R. Klosowski, D. Wolters, S. Brunner, W.-M. Franz, et al. (2013)
FASEB J 27, 4108-4121
   Abstract »    Full Text »    PDF »
The Serum- and Glucocorticoid-inducible Kinases SGK1 and SGK3 Regulate hERG Channel Expression via Ubiquitin Ligase Nedd4-2 and GTPase Rab11.
S. M. Lamothe and S. Zhang (2013)
J. Biol. Chem. 288, 15075-15084
   Abstract »    Full Text »    PDF »
Neurotrophic Effects of Serum- and Glucocorticoid-Inducible Kinase on Adult Murine Mesencephalic Dopamine Neurons.
X. Chen, P. Tagliaferro, T. Kareva, O. Yarygina, N. Kholodilov, and R. E. Burke (2012)
J. Neurosci. 32, 11299-11308
   Abstract »    Full Text »    PDF »
mSIN1 Protein Mediates SGK1 Protein Interaction with mTORC2 Protein Complex and Is Required for Selective Activation of the Epithelial Sodium Channel.
M. Lu, J. Wang, H. E. Ives, and D. Pearce (2011)
J. Biol. Chem. 286, 30647-30654
   Abstract »    Full Text »    PDF »
Serum- and glucocorticoid-inducible kinase 1 (SGK1) controls Notch1 signaling by downregulation of protein stability through Fbw7 ubiquitin ligase.
J.-S. Mo, E.-J. Ann, J.-H. Yoon, J. Jung, Y.-H. Choi, H.-Y. Kim, J.-S. Ahn, S.-M. Kim, M.-Y. Kim, J.-A. Hong, et al. (2011)
J. Cell Sci. 124, 100-112
   Abstract »    Full Text »    PDF »
The Stress Hormone Corticosterone Increases Synaptic {alpha}-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors via Serum- and Glucocorticoid-inducible Kinase (SGK) Regulation of the GDI-Rab4 Complex.
W. Liu, E. Y. Yuen, and Z. Yan (2010)
J. Biol. Chem. 285, 6101-6108
   Abstract »    Full Text »    PDF »
An amphipathic helix targets serum and glucocorticoid-induced kinase 1 to the endoplasmic reticulum-associated ubiquitin-conjugation machinery.
M. F. Arteaga, L. Wang, T. Ravid, M. Hochstrasser, and C. M. Canessa (2006)
PNAS 103, 11178-11183
   Abstract »    Full Text »    PDF »
Sgk3 links growth factor signaling to maintenance of progenitor cells in the hair follicle.
L. Alonso, H. Okada, H. A. Pasolli, A. Wakeham, A. I. You-Ten, T. W. Mak, and E. Fuchs (2005)
J. Cell Biol. 170, 559-570
   Abstract »    Full Text »    PDF »
Distribution and regulation of expression of serum- and glucocorticoid-induced kinase-1 in the rat kidney.
D. A. de la Rosa, T. Coric, N. Todorovic, D. Shao, T. Wang, and C. M Canessa (2003)
J. Physiol. 551, 455-466
   Abstract »    Full Text »    PDF »

To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882