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Its enzymatic activity is mediated by various signals, and it acts as a sensor of cellular NADP+ levels (Fig. 3).
AMP-activated protein kinase (AMPK) phosphorylation, a sensor of cellular energy status, directs metabolic adaptation to support cellular growth and survival after CCH.
AMPK was first discovered as a sensor of cellular energy status in all eukaryotic cells.
AMPK is the downstream component of a kinase cascade that acts as a sensor of cellular energy charge, being activated by rising AMP coupled with falling ATP.
AMPK is the downstream component of a pathway that acts as a sensor of cellular energy charge by monitoring AMP∶ATP ratio.
High ATP content, a reflection of high cellular energy status, will antagonize the binding of AMP to the gamma-subunit, and this allows the system to act as a sensor of cellular energy status [12].
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Previous research suggests that metformin may be involved in the tumor suppressor pathway by indirectly activating AMP-activated protein kinase (9)—a key sensor of cellular ATP and AMP balance and plays a role on activating tumor suppressor genes, e.g., LKB1.
Previous studies have suggested that AMPK activation, a sensor of the cellular energy status, stimulates autophagy via AMPK-mediated phosphorylation of ULK-1.
This rne 5'UTR element acts as a sensor of the cellular RNase E concentration and allows for auto-regulation of its mRNA degradation [ 59].
AMP-activated protein kinase (AMPK) is a serine/threonine protein kinase that acts as a master sensor of cellular energy balance in mammalian cells by regulating glucose and lipid metabolism [ 34].
AMPK α is a prominent sensor of cellular energy status, which acts as a marker of the level of intercellular ATP pool.
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