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Literature summary for 2.7.11.31 extracted from

  • Alesutan, I.; Foeller, M.; Sopjani, M.; Dermaku-Sopjani, M.; Zelenak, C.; Froehlich, H.; Velic, A.; Fraser, S.; Kemp, B.E.; Seebohm, G.; Voelkl, H.; Lang, F.
    Inhibition of the heterotetrameric K+ channel KCNQ1/KCNE1 by the AMP-activated protein kinase (2011), Mol. Membr. Biol., 28, 79-89.
    View publication on PubMed
Search for more literature for 2.7.11.31

Activating Compound

Activating Compound Comment Organism Structure
5-aminoimidazole-4-carboxamide ribonucleotide i.e. AICAR, activation of AMPK in isolated perfused proximal renal tubules by AICAR Homo sapiens
AMP
-
 Homo sapiens
additional information ischemia stimulates the AMP-activated protein kinase (AMPK) Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
wild-type HA-tagged AMPKalpha1, FLAG-tagged AMPKbeta1, HA-tagged AMPKgamma1, constitutively active HA-tagged AMPKgamma1 mutant R70Q , kinase dead mutant HA-tagged AMPKalpha1 mutant K45R, and wild type HA-tagged AMPK alpha2, recombinant expression in Xenopus laevis oocytes. Coexpression with human KCNQ1/KCNE1. AMPK inhibites voltage-gated outward currents in KCNQ1/KCNE1-expressing Xenopus oocytes. Coexpression of the AMP-activated protein kinase, i.e. AMPKalpha1, AMPKbeta1, and AMPKgamma1 Homo sapiens

Protein Variants

Protein Variants Comment Organism
K45R site-directed mutagenesis, a kinase dead mutant AMPK, the mutant is ineffective in inhibiting heterotetrameric K+-channel KCNQ1/KCNE1 Homo sapiens
R70Q site-directed mutagenesis, the constitutively active mutant is more effective in inhibiting heterotetrameric K+-channel KCNQ1/KCNE1 than the wild-type enzyme Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
compound C
-
 Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
 Homo sapiens 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + ubiquitin ligase Nedd4-2 Homo sapiens activation ADP + phosphorylated ubiquitin ligase Nedd4-2
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q13131 AND Q9Y478 AND P54619 AMPKalpha1, AMPKbeta1, and AMPKgamma1
-

Source Tissue

Source Tissue Comment Organism Textmining
epithelium
-
 Homo sapiens
-
heart
-
 Homo sapiens
-
liver
-
 Homo sapiens
-
renal proximal tubule
-
 Homo sapiens
-
skeletal muscle
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + ubiquitin ligase Nedd4-2
-
 Homo sapiens ADP + phosphorylated ubiquitin ligase Nedd4-2
-
 ?
ATP + ubiquitin ligase Nedd4-2 activation Homo sapiens ADP + phosphorylated ubiquitin ligase Nedd4-2
-
 ?

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Homo sapiens

General Information

General Information Comment Organism
physiological function ischemia stimulates the AMP-activated protein kinase (AMPK), a serine/threonine kinase, sensing energy depletion and stimulating several cellular mechanisms to enhance energy production and to limit energy utilization. AMPK downregulates the epithelial Na+ channel ENaC mediated by the ubiquitin ligase Nedd4-2. AMPK regulates the heterotetrameric K+-channel KCNQ1/KCNE1. Wild-type and constitutively active AMPK significantly reduce KCNQ1/KCNE1-mediated currents and reduce KCNQ1 abundance in the cell membrane of transfected Xenopus laevis oocytes, overview. AMPK decreased the KCNQ1 protein abundance in the cell membrane via ubiquitin ligase Nedd4-2 Homo sapiens