Literature summary for 2.7.11.1 extracted from

Matheny, R.W.; Geddis, A.V.; Abdalla, M.N.; Leandry, L.A.
Phosphatidylinositol 3-kinase p110alpha mediates phosphorylation of AMP-activated protein kinase in myoblasts (2016), Biochem. Biophys. Res. Commun., 469, 1117-1122.

Search for more literature for 2.7.11.1

Activating Compound

Activating Compound	Comment	Organism	Structure
additional information	p110alpha-mediated phosphorylation of AMPKa at S485/491 is Akt-dependent	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
recombinant expression of wild-type and mutant enzymes in Spodoptera frugiperda Sf9 cells using the baculovirus transfection method	Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
E545K	site-directed mutagenesis	Homo sapiens
K802R	site-directed mutagenesis	Homo sapiens
additional information	enzyme silencing by siRNA directed against p110alpha, or overexpression of constitutively-active or dominant negative p110alpha	Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
additional information	the p110alpha-mediated increase in AMPK S485/491 phosphorylation is eliminated in the presence of the Akt inhibitor MK2206	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cell membrane	the enzyme subunits are recruited to the cell membrane following activation of receptor tyrosine kinases and G protein-coupled receptors	Homo sapiens	-	-

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
85000	-	-	Homo sapiens
110000	-	-	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + AMP-activated protein kinase alpha1	Homo sapiens	phosphorylation of Ser485 at subunit alpha1 and of Ser491 at subunit alpha2	ADP + phospho-AMP-activated protein kinase	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P42336	subunit p110alpha	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	the enzyme subunits are recruited to the cell membrane following activation of receptor tyrosine kinases and G protein-coupled receptors	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
C2C12 cell	-	Homo sapiens	-
skeletal muscle	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + AMP-activated protein kinase alpha1	phosphorylation of Ser485 at subunit alpha1 and of Ser491 at subunit alpha2	Homo sapiens	ADP + phospho-AMP-activated protein kinase	-	?
additional information	the enzyme does not phosphorylate Thr172, but suppresses its phosphorylation	Homo sapiens	?	-	?

Subunits

Subunits	Comment	Organism
heterodimer	1 * 110000, p110 subunit, + 1 * 85000, p85 subunit	Homo sapiens
More	class IA PI3K enzymes are composed of an 85 kDa regulatory subunit (p85) and a 110 kDa catalytic subunit (p110)	Homo sapiens

Synonyms

Synonyms	Comment	Organism
phosphatidylinositol 3-kinase	-	Homo sapiens
PI3K	-	Homo sapiens

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Homo sapiens

General Information

General Information	Comment	Organism
malfunction	chemical inhibition, siRNA, and expression of dominant-negative p110alpha are all associated with increased AMPK T172 phosphorylation, whereas expression of constitutively-active p110alpha reduces T172 phosphorylation. Pharmacological inhibition of p110a reduces AMPK S485/491 phosphorylation, while constitutively-active p110alpha increases AMPK S485/491 phosphorylation. In response to oligomycin or serum starvation, AMPK T172 phosphorylation is elevated in p110alpha-deficient myoblasts compared to control myoblasts. p110alpha deficiency modifies AMPK responses to cellular stress	Homo sapiens
physiological function	AMP-activated protein kinase (AMPK) is a serine/threonine kinase that functions as a sensor of intracellular energy. Activation of AMPK is associated with increased phosphorylation of the alpha-subunit at threonine 172 and decreased phosphorylation at serine 485 in AMPKalpha1 and serine 491 in AMPKalpha2 (S485/491). p110alpha-mediated phosphorylation of AMPKa at S485/491 is Akt-dependent	Homo sapiens

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Release 2023.1 (January 2023)