Hyperosmotic stress stimulates promoter activity and regulates cellular utilization of the serum- and glucocorticoid-inducible protein kinase (Sgk) by a p38 MAPK-dependent pathway (Q30876351)

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English	Hyperosmotic stress stimulates promoter activity and regulates cellular utilization of the serum- and glucocorticoid-inducible protein kinase (Sgk) by a p38 MAPK-dependent pathway	scientific article

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scholarly article

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Europe PubMed Central

27 June 2017

Hyperosmotic stress stimulates promoter activity and regulates cellular utilization of the serum- and glucocorticoid-inducible protein kinase (Sgk) by a p38 MAPK-dependent pathway (English)

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Europe PubMed Central

27 June 2017

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Europe PubMed Central

27 June 2017

6

object named as

B A Hemmings

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Europe PubMed Central

27 June 2017

author name string

L M Bell

1

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Europe PubMed Central

27 June 2017

M L Leong

2

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Europe PubMed Central

27 June 2017

B Kim

3

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Europe PubMed Central

27 June 2017

E Wang

4

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Europe PubMed Central

27 June 2017

G L Firestone

7

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Europe PubMed Central

27 June 2017

language of work or name

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publication date

1 August 2000

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Europe PubMed Central

27 June 2017

Journal of Biological Chemistry

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Europe PubMed Central

27 June 2017

275

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Europe PubMed Central

27 June 2017

33

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Europe PubMed Central

27 June 2017

25262-25272

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Europe PubMed Central

27 June 2017

Protein kinase cascades activated by stress and inflammatory cytokines

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Expression of the glyoxalase I gene of Saccharomyces cerevisiae is regulated by high osmolarity glycerol mitogen-activated protein kinase pathway in osmotic stress response.

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Different signalling pathways contribute to the control of GPD1 gene expression by osmotic stress in Saccharomyces cerevisiae

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GPD1, which encodes glycerol-3-phosphate dehydrogenase, is essential for growth under osmotic stress in Saccharomyces cerevisiae, and its expression is regulated by the high-osmolarity glycerol response pathway

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Mitogen and stress response pathways: MAP kinase cascades and phosphatase regulation in mammals and yeast

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The stress-activated protein kinase pathways

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Organization and regulation of mitogen-activated protein kinase signaling pathways

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Characterization of sgk, a novel member of the serine/threonine protein kinase gene family which is transcriptionally induced by glucocorticoids and serum

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Serum and glucocorticoid-inducible kinase (SGK) is a target of the PI 3-kinase-stimulated signaling pathway

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p53 stimulates promoter activity of the sgk. serum/glucocorticoid-inducible serine/threonine protein kinase gene in rodent mammary epithelial cells

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Differential expression of sgk mRNA, a member of the Ser/Thr protein kinase gene family, in rat brain after CNS injury.

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Osmotic shock inhibits insulin signaling by maintaining Akt/protein kinase B in an inactive dephosphorylated state

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Inactivation and dephosphorylation of protein kinase Balpha (PKBalpha) promoted by hyperosmotic stress

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Osmotic stress inhibits p70/85 S6 kinase through activation of a protein phosphatase

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sgk is an aldosterone-induced kinase in the renal collecting duct. Effects on epithelial na+ channels.

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Shear stress induction of the tissue factor gene

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Protein kinase B/Akt participates in GLUT4 translocation by insulin in L6 myoblasts

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Insulin stimulation of the fatty acid synthase promoter is mediated by the phosphatidylinositol 3-kinase pathway. Involvement of protein kinase B/Akt

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Glucose or diabetes activates p38 mitogen-activated protein kinase via different pathways

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Hyperglycemia inhibits insulin activation of Akt/protein kinase B but not phosphatidylinositol 3-kinase in rat skeletal muscle.

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Identifiers

10.1074/JBC.M002076200

1 reference

Europe PubMed Central

27 June 2017

1 reference

Europe PubMed Central

27 June 2017

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