K+ channel activation by all three isoforms of serum- and glucocorticoid-dependent protein kinase SGK

  title={K+ channel activation by all three isoforms of serum- and glucocorticoid-dependent protein kinase SGK},
  author={Nikita Gamper and Sophie A. Fillon and Y. Feng and Bj{\"o}rn Friedrich and Paul Lang and Guido Henke and Stephan M Huber and T. Kobayashi and Philip Cohen and Florian Lang},
  journal={Pfl{\"u}gers Archiv},
Abstract. The serum- and glucocorticoid-dependent kinase SGK1 was originally identified as a glucocorticoid-sensitive gene. Subsequently, the two homologous kinases SGK2 and SGK3 have been cloned, being products of distinct genes, which are differentially expressed and share 80% identity in amino acid sequence in their catalytic domains. While SGK1 has been shown to activate ion channels, including K+ channels, the functions of SGK2 and SGK3 have not been examined. The present study was… 
(Patho)physiological significance of the serum- and glucocorticoid-inducible kinase isoforms.
The serum- and glucocorticoid-inducible kinase-1 (SGK1) is ubiquitously expressed and under genomic control by cell stress and hormones, and may play an active role in a multitude of pathophysiological conditions.
Regulation of Channels by the Serum and Glucocorticoid-Inducible Kinase - Implications for Transport, Excitability and Cell Proliferation
The serum and glucocorticoid-inducible kinase SGK1 stimulates the Na+ channels ENaC and SCN5A, the K+ channels ROMK1, Kv1.3, and KCNE1/KCNQ1, the cation conductance induced by 4F2/LAT1 and the
Serum- and glucocorticoid-inducible kinase 1 (SGK1) mediates glucocorticoid-induced inhibition of insulin secretion.
It is shown that dexamethasone upregulates transcription and expression of the serum- and glucocorticoid-inducible kinase 1 (SGK1) in insulin-secreting cells, an effect reversed by mifepristone (RU486), an antagonist of the nuclear glucoc Corticoid receptor.
Serum- and glucocorticoid-inducible kinase 1 in the regulation of renal and extrarenal potassium transport
SGK1-dependent regulation of K+ channels and K+ transport contributes to the stimulation of renal K+ excretion following high K+ intake, to insulin-induced cellular K+ uptake and hypokalemia, to inhibition of insulin release by glucocorticoids, to stimulation of mast cell degranulation and gastric acid secretion, and to cardiac repolarization.
Regulation of KCNE1-dependent K+ current by the serum and glucocorticoid-inducible kinase (SGK) isoforms
All three members of the SGK family of kinases SGK1–3 and protein kinase B stimulate the slowly activating K+ channel KCNE1/KCNQ1 and the kinases may participate in the regulation ofKCNE1-dependent transport and excitability.
Stimulation of the EAAT4 glutamate transporter by SGK protein kinase isoforms and PKB.
Role of the serum and glucocorticoid inducible kinase SGK1 in glucocorticoid stimulation of gastric acid secretion
SGK1 is not required for basal and cyclic AMP-stimulated gastric H+ secretion but participates in the stimulation of gastricH+ secretion by glucocorticoids and may involve stimulation of K+ channels.
Deranged Kv channel regulation in fibroblasts from mice lacking the serum and glucocorticoid inducible kinase SGK1
In conclusion, lack of SGK1 does not abrogate Kv channel activity but abolishes regulation of those channels by serum, glucocorticoid and IGF‐1, an effect influencing capacitative Ca2+ entry in sgk1+/+ MTF, whereas in s gk1−/− cells it remained unchanged.
Additive regulation of GluR1 by stargazin and serum- and glucocorticoid-inducible kinase isoform SGK3
SGK3 and stargazin regulate GluR1 independently, and thus, their effects on glutamate-induced currents are additive.


Characterization of the structure and regulation of two novel isoforms of serum- and glucocorticoid-induced protein kinase.
Two novel isoforms of SGK are identified, termed SGK2 and SGK3, whose catalytic domains share 80% amino acid sequence identity with each other and with SGK (renamed SGK1), and are activated in vitro by PDK1 and in vivo in response to signals that activate phosphatidylinositol (PI) 3-kinase.
The Serum and Glucocorticoid Kinase sgk Increases the Abundance of Epithelial Sodium Channels in the Plasma Membrane of Xenopus Oocytes*
The experiments indicate that sgk stimulates electrogenic sodium transport by increasing the number of ENaCs at the cell surface and suggest that s gk may mediate the early increase in aldosterone-induced sodium current.
Characterization of sgk, a novel member of the serine/threonine protein kinase gene family which is transcriptionally induced by glucocorticoids and serum.
This is the first report of a presumed serine/threonine protein kinase that is highly regulated at the transcriptional level by glucocorticoid hormones and suggests a novel interplay between glucoc Corticoid receptor signalling and aprotein kinase of the second messenger family.
sgk Is an Aldosterone-induced Kinase in the Renal Collecting Duct
It is reported here that aldosterone rapidly increases mRNA levels of a putative Ser/Thr kinase,sgk (or serum- andglucocorticoid-regulated kinase), in its native target cells, i.e. in cortical collecting duct cells, and this protein kinase plays an important role in the early phase of ald testosterone-stimulated Na+ transport.
Epithelial sodium channel regulated by aldosterone-induced protein sgk.
Sgk (serum and glucocorticoid-regulated kinase), a member of the serine-threonine kinase family, is identified as an aldosterone-induced regulator of ENaC activity, suggesting that sgk plays a central role in ald testosterone regulation of Na+ absorption and thus in the control of extracellular fluid volume, blood pressure, and sodium homeostasis.
Serum and Glucocorticoid-regulated Kinase Modulates Nedd4-2-mediated Inhibition of the Epithelial Na+Channel*
SGK regulates epithelial Na+ absorption in part by modulating the function of hNedd4-2 by phosphorylation and a PY motif in SGK mediated the interaction and was required for SGK to stimulate ENaC.
Cloning and characterization of a putative human serine/threonine protein kinase transcriptionally modified during anisotonic and isotonic alterations of cell volume.
The putative serine/threonine protein kinase h-sgk may provide a functional link between the cellular hydration state and metabolic control.
Cerebral localization and regulation of the cell volume-sensitive serum- and glucocorticoid-dependent kinase SGK1
Co-expression studies in Xenopus laevis oocytes revealed that SGK1 markedly increased the activity of the neuronal K+ channel Kv1.3 as activation of K+ channels modifies excitation of neuronal cells,SGK1 may participate in the regulation of neuronal excitability.
IGF-1 up-regulates K+ channels via PI3-kinase, PDK1 and SGK1
In conclusion, IGF-1 through PI3-kinase, PDK1 and SGK1 up-regulates Kv channels, an effect required for the proliferative action of the growth factor.
Heterologous expression of specific K+ channels in T lymphocytes: functional consequences for volume regulation.
  • C. DeutschL. Chen
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1993
It is shown that a mouse cytotoxic T-lymphocyte line, CTLL-2, is devoid of voltage-dependent K+ channels and is unable toVolume regulate, and transient transfection of these cells with Kv1.3 reconstitutes their ability to volume regulate.