Related Experiment Video
Updated: Aug 19, 2026

Induction and Analysis of Epithelial to Mesenchymal Transition
Published on: August 27, 2013
Serum/glucocorticoid-inducible kinase can phosphorylate the cyclic AMP response element binding protein, CREB
1Children's Hospital of Philadelphia, Joseph Stokes Jr. Research Institute, ARC 814, 3615 Civic Center Boulevard, Philadelphia, PA 19104, USA.
Abstract:
To maintain homeostasis, cells often respond to stressful extra-cellular stimuli by new gene expression. Serum/glucocorticoid-induced kinase (SGK) is an immediate early gene whose expression is induced by a variety of extra-cellular stimuli. Here, we examine the possibility that SGK can directly phosphorylate the transcription factor cyclic AMP response element binding protein (CREB). In a cell-free context, SGK physically associates with CREB and SGK phosphorylates it on serine 133. Phospho-serine 133 is essential for stimulating the transcriptional activity of CREB. Further, we show that in a variety of cellular contexts, SGK phosphorylates CREB. Activation of receptor tyrosine kinase pathways or the phosphoinositide-dependent kinase 1 (PDK1) lead to SGK-dependent CREB phosphorylation. Hormonal stimulation of epithelial cells leads to the induction of endogenous SGK and CREB phosphorylation. A dominant-negative form of SGK blocks dexamethasone-induced CREB phosphorylation. Our studies indicate that stimulation of SGK can lead to CREB phosphorylation, suggesting that CREB-dependent gene transcription is an important link between stressful extra-cellular signals and cellular responses.
More Related Videos
Related Concept Videos
cAMP-dependent Protein Kinase Pathways
Calmodulin-dependent Signaling
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Amplifying Signals via Enzymatic Cascade
Cell Specific Gene Expression
MAPK Signaling Cascades
TGF - β Signaling Pathway

