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Cited by 139Ion Transport and Channel RegulationRenin-Angiotensin System StudiesChronic Kidney Disease and Diabetes

The physiological impact of the serum and glucocorticoid-inducible kinase SGK1

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Lang, Florian, Artunc, Ferruh, Vallon, Volker·2009·Current Opinion in Nephrology and Hypertension
DOI 10.1097/mnh.0b013e32832f125ePMC PMC2883450
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Abstract

PURPOSE OF REVIEW: The role of serum and glucocorticoid-inducible kinase 1 (SGK1) in renal physiology and pathophysiology is reviewed with particular emphasis on recent advances. RECENT FINDINGS: The mammalian target of rapamycin complex 2 has been shown to phosphorylate SGK1 at Ser422 (the so-called hydrophobic motif). Ser397 and Ser401 are two additional SGK1-phosphorylation sites required for maximal SGK1 activity. A 5' variant alternate transcript of human Sgk1 has been identified that is widely expressed and shows improved stability, enhanced membrane association, and greater stimulation of epithelial Na+ transport. SGK1 is essential for optimal processing of the epithelial sodium channel and also regulates the expression of the Na+-Cl- cotransporter. With regard to pathophysiology, SGK1 participates in the stimulation of renal tubular glucose transport in diabetes, the renal profibrotic effect of both angiotensin II and aldosterone, and in fetal programing of arterial hypertension. SUMMARY: The outlined recent findings advanced our understanding of the molecular regulation of SGK1 as well as the role of the kinase in renal physiology and the pathophysiology of renal disease and hypertension. Future studies using pharmacological inhibitors of SGK1 will reveal the utility of the kinase as a new therapeutic target.

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  • Increased cytosolic Ca2+ activity and NO are among the regulators that control SGK1 transcription.

    “SGK1 transcription is controlled by a wide variety of additional hormones and further regulators including increase of cytosolic Ca 2+ activity and NO (Lang et al. 2006(Lang et al. , 2009)).”

    From Significance of SGK1 in the regulation of neuronal function (2010) · cites this paper as Lang et al. , 2009

    The Introduction and “Regulation of SGK1 expression and activity” section say that many stimuli control SGK1 transcription. But the section describes increased cytosolic Ca2+ as activating SGK1, not controlling its transcription; the passages about NO describe SGK1 affecting nitric oxide production, not NO regulating SGK1 transcription. No page numbers are available in our copy. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

  • SGK1 contributes to the regulation of transport, hormone release, neuroexcitability, inflammation, cell proliferation and apoptosis.

    “SGK1 contributes to the regulation of transport, hormone release, neuroexcitability, inflammation, cell proliferation and apoptosis (Lang et al. 2006(Lang et al. , 2009)).”

    From Significance of SGK1 in the regulation of neuronal function (2010) · cites this paper as Lang et al. , 2009

    The Conclusions (page unavailable) say SGK1 participates in regulating epithelial transport, excitability, cell proliferation and apoptosis, and plays a role in inflammation. Our copy does not establish that SGK1 regulates hormone release; it also does not specify that the excitability mentioned is neuronal. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

  • SGK1 is involved in the pathophysiology of neurodegeneration.

    “SGK1 is further involved in the pathophysiology of allergy, peptic ulcer, tumour growth, fibrosing disease, ischaemia and neurodegeneration (Lang et al. 2006(Lang et al. , 2009)).”

    From Significance of SGK1 in the regulation of neuronal function (2010) · cites this paper as Lang et al. 2009

    The section on SGK1-dependent cellular functions says SGK1 phosphorylates tau and huntingtin, but adds that the functional significance of such phosphorylation is usually unclear. The References section also lists a study associating sgk1 with cell death in a model of Parkinson’s disease. These passages connect SGK1 to neurodegeneration-related proteins and a disease model, but do not establish its involvement in the pathophysiology of neurodegeneration. (LLM, conf=0.81)

    Experimental — accuracy not yet measured

  • SGK1 increases the protein abundance and/or activity of a variety of ion channels, carriers, and the Na+/K+-ATPase.

    “SGK1 increases the protein abundance and/or activity of a variety of ion channels (e.g.SCN5A, ENaC, ASIC1, TRPV5,6, ROMK, Kv1.1-5, KCNE1/KCNQ1, KCNQ2-5, GluR6, VSOAC, ClC2, CFTR), carriers (e.g.NHE3, NKCC2, NCC, NaPiIIb, SMIT, GLUT1,4, SGLT1, NaDC, EAAT1-5, SN1, ASCT2, 4F2/LAT, PepT2, CreaT), and the Na + /K + -ATPase”

    From Significance of SGK1 in the regulation of neuronal function (2010) · cites this paper as Lang et al. , 2009

  • SGK1 is activated by insulin and growth factors via PI3-kinase, PDK1, and mTORC2.

    “The kinase is activated by insulin and growth factors via PI3-kinase, the 3-phosphoinositide-dependent kinase PDK1, and the mammalian target of rapamycin mTORC2 (Lang et al. 2006(Lang et al. , 2009;;Peterson et al. 2009).”

    From Significance of SGK1 in the regulation of neuronal function (2010) · cites this paper as Lang et al. , 2009

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Cited by

Sorted by citations

Authors
Lang, F., Artunc, F., & Vallon, V.
Affiliations
  • University of Tübingen (DE)
  • University of California San Diego (US)
Corresponding author
Lang, Florian
ORCID
Venue
Current Opinion in Nephrology and Hypertension
Publisher
Ovid Technologies (Wolters Kluwer Health)
Published
2009-09
Volume
18
Issue
5
Pages
439-448
ISSN
1062-4821 (ISSN-L)
DOI
10.1097/mnh.0b013e32832f125e
PMC
PMC2883450
OpenAlex
W2075971181
Cited by
139
References
3
Citations by year
2026: 3 · 2025: 3 · 2024: 3 · 2023: 6 · 2022: 5 · 2021: 12 · 2020: 8 · 2019: 6 · 2018: 8 · 2017: 10 · 2016: 8 · 2015: 15 · 2014: 13 · 2013: 7 · 2012: 11
FWCI
0.82
Type
journal article
Language
en
Open access
Locations
  • Current Opinion in Nephrology & Hypertension (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
Funders
  • National Institutes of Health
  • National Institute of Diabetes and Digestive and Kidney Diseases (R01 DK-56248, R01DK028602, P30DK079337, R01DK056248)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion Transport and Channel Regulation
  • Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Renin-Angiotensin System Studies
  • Health Sciences › Medicine › Nephrology › Chronic Kidney Disease and Diabetes
Keywords
SGK1, serum- and glucocorticoid-inducible kinase, renal physiology, mTORC2, protein phosphorylation, epithelial sodium channel, NaCl cotransporter, diabetic nephropathy, renal fibrosis, angiotensin II, aldosterone, SGK1 inhibitor, therapeutic target
MeSH terms
Serum-Glucocorticoid Regulated Kinases, Animals, Appetite, Humans, Hypertension, Kidney, Obesity, Gene Expression Regulation, Enzymologic, Protein Serine-Threonine Kinases, Immediate-Early Proteins, Metabolic Syndrome

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