SIK is a protein kinase that is involved in regulating AMPK-related kinases. SIK may mediate the physiological effects of LKB1, including its tumour suppressor function. SIK is also involved in signaling by various proteins like STRAD, NUAK1, NUAK2, BRSK1, BRSK2, QIK, QSK, SIK, MARK1, MARK2, MARK3, MARK4 and MELK that are related to AMPK. Activation of SIK1 by phosphorylation on thr322 can lead to an increase in the catalytic activity of sodium/potassium ATPase alpha subunit at the plasma membrane. This results in an increase in intracellular sodium in intact mammalian cells.
The transcription factor cAMP response element-binding protein (CREB) plays important roles in gene expression induced by cAMP signaling and is believed to be activated when its Ser133 is phosphorylated. However, the discovery of Ser133-independent activation by the activation of transducer
Proceedings of the National Academy of Sciences of the United States of America, 104(43), 16922-16927 (2007-10-18)
In mammalian cells, active sodium transport and its derived functions (e.g., plasma membrane potential) are dictated by the activity of the Na(+),K(+)-ATPase (NK), whose regulation is essential for maintaining cell volume and composition, as well as other vital cell functions.
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