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PMID |
Sentence |
1 |
15068958
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Contraction, phenformin, or AICAR did not significantly increase activities or expression of the AMPK-related kinases QSK, QIK, MARK2/3, and MARK4 in skeletal muscle.
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2 |
17805301
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Insulin disrupts TORC2 activity by induction of the Ser/Thr kinase SIK2, which we show here undergoes AKT2-mediated phosphorylation at Ser 358.
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3 |
17805301
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Activated SIK2 in turn stimulated the Ser 171 phosphorylation and cytoplasmic translocation of TORC2.
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4 |
18239551
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Electroporation was used to transiently transfect 3T3-L1 adipocytes with fatty acid synthase (FAS) promoter-driven luciferase construct to evaluate the effect of SIK2 on FAS transcription.
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5 |
18239551
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Overexpression of SIK2 repressed the expression of lipogenic genes, including FAS, acetyl CoA carboxylase 2 (ACC2), and stearoyl CoA desaturase 1 (SCD1), and reduced triglyceride content.
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6 |
18239551
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Reduction of endogenous SIK2 expression through RNA interference increased the expression of FAS, ACC2, and SCD1.
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7 |
18239551
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This effect is independent of adenosine monophosphate-activated protein kinase (AMPK) since neither phosphorylation state nor protein level of AMPKalpha1 and AMPKalpha2 was affected by SIK2 overexpression.
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8 |
18239551
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SIK2 inhibits the expression of FAS-promoter driven luciferase reporter gene, and this effect can be reversed by overexpression of constitutively active sterol regulatory element binding protein-1 (SREBP-1).
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9 |
18239551
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Furthermore, SIK2 also reduces the nuclear translocation of endogenous SREBP-1.
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10 |
21084751
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In this study, we have identified the histone acetyltransferase (HAT) coactivator p300 and serine/threonine kinase salt-inducible kinase 2 (SIK2) as key upstream regulators of ChREBP activity.
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11 |
21084751
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SIK2 inhibited p300 HAT activity by direct phosphorylation on Ser89, which in turn decreased ChREBP-mediated lipogenesis in hepatocytes and mice overexpressing SIK2.
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12 |
21084751
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Finally, in mouse models of type 2 diabetes and obesity, low SIK2 activity was associated with increased p300 HAT activity, ChREBP hyperacetylation, and hepatic steatosis.
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