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Literature summary for 2.7.1.151 extracted from

  • Bang, S.; Kim, S.; Dailey, M.J.; Chen, Y.; Moran, T.H.; Snyder, S.H.; Kim, S.F.
    AMP-activated protein kinase is physiologically regulated by inositol polyphosphate multikinase (2012), Proc. Natl. Acad. Sci. USA, 109, 616-620.
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Mus musculus
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Posttranslational Modification

Posttranslational Modification Comment Organism
phosphoprotein glucose activates phosphorylation of IPMK at residue Tyr174 enabling the enzyme to bind to AMP-activated kinase and regulate its activation Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
hypothalamus
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 Mus musculus
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Subunits

Subunits Comment Organism
More IPMK physiologically binds AMP-activated kinase, with binding enhanced by glucose treatment Mus musculus

General Information

General Information Comment Organism
physiological function inositol polyphosphate multikinase IPMK regulates glucose signaling to AMP-activated kinase in a pathway whereby glucose activates phosphorylation of IPMK at residue Tyr174 enabling the enzyme to bind to AMP-activated kinase and regulate its activation. Refeeding fasted mice rapidly and markedly stimulates transcriptional enhancement of IPMK expression while down-regulating AMP-activated kinase. AMP-activated kinase is up-regulated in mice with genetic depletion of hypothalamic IPMK. IPMK physiologically binds AMP-activated kinase, with binding enhanced by glucose treatment. Regulation by glucose of phospho-AMP-activated kinase in hypothalamic cell lines is prevented by blocking AMP-activated kinase-IPMK binding Mus musculus