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Literature summary for 2.7.11.31 extracted from

  • Chen, M.; Liu, J.; Yang, L.; Ling, W.
    AMP-activated protein kinase regulates lipid metabolism and the fibrotic phenotype of hepatic stellate cells through inhibition of autophagy (2017), FEBS Open Bio, 7, 811-820 .
    View publication on PubMedView publication on EuropePMC
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Activating Compound

Activating Compound Comment Organism Structure
5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranoside
-
 Homo sapiens
metformin
-
 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein the enzyme can be activated by direct phosphorylation by the upstream kinase liver kinase B1 at the site of Thr172 on the alpha-subunit, or through indirect allosteric changes of the gamma-subunit, thereby regulating the phosphorylation state of the alpha-subunit Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
hepatic stellate cell
-
 Homo sapiens
-
LX-2 cell
-
 Homo sapiens
-

Synonyms

Synonyms Comment Organism
AMP-activated protein kinase
-
 Homo sapiens
AMPK
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function enzyme phosphorylation inhibits the activation of human hepatic stellate cell line LX-2. Enzyme activation in LX-2 cells inhibits autophagosome formation. Enzyme activation inhibits transforming growth factor-beta-induced intracellular lipid droplet depletion, which relies on increased autophagic flux, and finally inhibits transforming growth factor-beta-induced hepatic stellate cell activation Homo sapiens