The node-based overlap between this network and other networks is calculated as the Szymkiewicz-Simpson coefficient of their respective nodes. Up to the top 10 are shown below.
|BEL Framework Large Corpus Document v20170611||40%|
|Hypoxic Stress-2.0-Hs v2.0||29%|
|Hypoxic Stress-2.0-Mm v2.0||28%|
|Osmotic Stress-2.0-Rn v2.0||25%|
|Endoplasmic Reticulum Stress-2.0-Rn v2.0||19%|
|Oxidative Stress-2.0-Rn v2.0||18%|
AMPK phosphorylates CFTR in vitro at two essential serines (Ser(737) and Ser(768)) in the R domain,
AMPK-dependent CFTR phosphorylation renders the channel resistant to activation by PKA and PKC without preventing phosphorylation by these kinases. We found that Ser768, a CFTR R domain residue considered to be an inhibitory PKA site, is the dominant site of AMPK phosphorylation in vitro. Ser-to-Ala mutation at this site enhanced baseline CFTR activity and rendered CFTR resistant to inhibition by AMPK
The phosphorylation of raptor by AMPK is required for the inhibition of mTORC1 and cell-cycle arrest induced by energy stress.
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