Negative charge at the consensus sequence for the serum- and glucocorticoid-inducible kinase, SGK1, determines pH sensitivity of the renal outer medullary K+ channel, ROMK1.

@article{Palmada2003NegativeCA,
  title={Negative charge at the consensus sequence for the serum- and glucocorticoid-inducible kinase, SGK1, determines pH sensitivity of the renal outer medullary K+ channel, ROMK1.},
  author={M{\`o}nica Palmada and Hamdy M. Embark and Amanda W. Wyatt and Christoph B{\"o}hmer and Florian Lang},
  journal={Biochemical and biophysical research communications},
  year={2003},
  volume={307 4},
  pages={
          967-72
        }
}
SPAK and OSR1 Dependent Down-Regulation of Murine Renal Outer Medullary K+ Channel ROMK1
TLDR
ROMK1 protein abundance and activity are down-regulated by SPAK and OSR1, and this study concludes that WNK kinases further regulate the renal outer medullary K+ channel ROMK1.
New insights into the role of serum- and glucocorticoid-inducible kinase SGK1 in the regulation of renal function and blood pressure
  • V. Vallon, F. Lang
  • Biology, Medicine
    Current opinion in nephrology and hypertension
  • 2005
TLDR
PPARγ activators may increase renal Na+ reabsorption by stimulating SGK1 and ENaC andSGK1 may affect renal transport mechanisms beyond Na+Reabsorption and K+ secretion in ASDN and may be relevant to the pathophysiology of hypertension and other diseases.
(Patho)physiological significance of the serum- and glucocorticoid-inducible kinase isoforms.
TLDR
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.
Serum- and glucocorticoid-inducible kinase 1 in the regulation of renal and extrarenal potassium transport
TLDR
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 ion channels by the serum‐ and glucocorticoid‐inducible kinase SGK1
  • F. Lang, E. Shumilina
  • Biology, Medicine
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 2013
TLDR
SGK1‐dependent ion channel regulation may become pathophysiologically relevant primarily after excessive (pathological) expression, and SGK1 may be considered an attractive therapeutic target despite its broad range of functions.
Phosphorylation-regulated endoplasmic reticulum retention signal in the renal outer-medullary K+ channel (ROMK).
TLDR
Evidence is presented that phosphorylation of S44 modulates channel expression by increasing its cell surface delivery consequent to suppression of a COOH-terminal ER retention signal in ROMK1, which could provide a pool of mature and properly folded channels for rapid delivery to the plasma membrane.
Hypotonic activation of volume-sensitive outwardly rectifying chloride channels in cultured PASMCs is modulated by SGK.
TLDR
Data indicate that the PI3K-SGK cascade is activated on hypotonic swelling of PASMCs and, in turn, affects downstream signaling molecules linked to activation of VSOACs.
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References

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The serum and glucocorticoid-inducible kinase SGK1 and the Na+/H+ exchange regulating factor NHERF2 synergize to stimulate the renal outer medullary K+ channel ROMK1.
TLDR
NHERF2 andSGK1 interact to enhance ROMK1 activity in large part by enhancing the abundance of channel protein within the cell membrane, which allows the integration of genomic regulation and activation of SGK1 and NHERf2 in the control of ROMK 1 activity and renal K(+) excretion.
Regulation of KCNE1-dependent K+ current by the serum and glucocorticoid-inducible kinase (SGK) isoforms
TLDR
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 Xenopus oocyte Na+,K+ATPase by the serum and glucocorticoid-dependent kinase sgk1
TLDR
Results of the present study point to an additional action of sgk1 that may participate in the regulation of renal tubular Na+ transport and may be involved in theregulation of Na+/K+-ATPase in extrarenal tissues.
Regulation of sgk by aldosterone and its effects on the epithelial Na(+) channel.
TLDR
regulation of sgk by aldosterone in native mammalian epithelia and its effect on ENaC are characterized to suggest that the response is mediated, at least in part, by occupancy of the mineralocorticoid receptor.
Effects of the Serine/Threonine Kinase SGK1 on the Epithelial Na+ Channel (ENaC) and CFTR: Implications for Cystic Fibrosis
TLDR
Enhanced expression of h-SGK1 in epithelial cells of CF-lung tissue may be a novel pathophysiological factor contributing to increased Na+ channel activity and thus to increasedNa+ transport in CF.
pH gating of ROMK (K(ir)1.1) channels: control by an Arg-Lys-Arg triad disrupted in antenatal Bartter syndrome.
  • U. Schulte, H. Hahn, J. Ludwig
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1999
TLDR
The results provide molecular understanding for normal pH gating of K(ir) channels as well as for the channel defects found in patients with antenatal Bartter syndrome.
PKA site mutations of ROMK2 channels shift the pH dependence to more alkaline values.
TLDR
The data are consistent with the hypothesis that in the native channel PKA activation involves a shift of the pK(a) value ofROMK channels to more acidic values, thus relieving a H(+)-mediated inhibition of ROMK channels.
pH-dependent modulation of the cloned renal K+ channel, ROMK.
TLDR
Intracellular acidification (pH 7.2) also increased the Mg-ATP binding affinity of ROMK2, resulting in a leftward shift of the relationship between ATP concentration and the reduction in channel activity, which could alter net charge and increase affinity for the negatively charged nucleotide.
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