NOK/STYK1 interacts with GSK-3β and mediates Ser9 phosphorylation through activated Akt (Q24299545)

2

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Feng Sheng

3

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Yi-Jia Li

4

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Da Jin

5

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Xue Ding

6

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Shuping Zhang

Cell signaling by receptor tyrosine kinases

7

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language of work or name

English

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publication date

2 November 2012

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published in

FEBS Letters

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volume

586

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page(s)

3787-92

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issue

21

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cites work

1 reference

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A novel protein tyrosine kinase NOK that shares homology with platelet- derived growth factor/fibroblast growth factor receptors induces tumorigenesis and metastasis in nude mice

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Diagnostic relevance of overexpressed mRNA of novel oncogene with kinase-domain (NOK) in lung cancers

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Aberrant STYK1 expression in ovarian cancer tissues and cell lines

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Point mutation at single tyrosine residue of novel oncogene NOK abrogates tumorigenesis in nude mice

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Functional regulation of Slug/Snail2 is dependent on GSK-3β-mediated phosphorylation.

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Dual regulation of Snail by GSK-3beta-mediated phosphorylation in control of epithelial-mesenchymal transition

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Metastasis and AKT activation

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Expression, localization, and activity of glycogen synthase kinase 3beta during mouse skin tumorigenesis.

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The phosphatidylinositol 3-Kinase AKT pathway in human cancer

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The role of glycogen synthase kinase 3 beta in the transformation of epidermal cells

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A common phosphate binding site explains the unique substrate specificity of GSK3 and its inactivation by phosphorylation

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Mouse 3-phosphoinositide-dependent protein kinase-1 undergoes dimerization and trans-phosphorylation in the activation loop

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Activation of phosphatidylinositol 3-kinase by membrane localization of p110alpha predisposes mammary glands to neoplastic transformation

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Mitogen inactivation of glycogen synthase kinase-3 beta in intact cells via serine 9 phosphorylation

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inferred from DOI database lookup

7 January 2021

based on heuristic

MicroRNAs differentially regulated by Akt isoforms control EMT and stem cell renewal in cancer cells.

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inferred from DOI database lookup

7 January 2021

based on heuristic

Membrane localization of phosphatidylinositol 3-kinase is sufficient to activate multiple signal-transducing kinase pathways

1 reference

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