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Literature summary for 2.7.11.11 extracted from

  • Shell, J.R.; Lawrence, D.S.
    Proteolytic regulation of the mitochondrial cAMP-dependent protein kinase (2012), Biochemistry, 51, 2258-2264.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.11.11

Activating Compound

Activating Compound Comment Organism Structure
calpain activates the PKA holoenzyme in a cAMP-independent fashion. A variety of agents, including inhibitors of the electron transport chain, activate calpain in a Ca2+-dependent manner, which, in turn, catalyzes the proteolysis of the R subunit, thereby releasing the C subunit in its active form, overview Bos taurus
cAMP exposure of mitochondria to cAMP results in enhanced catalytic subunit catalytic activity. Upon binding of cAMP to the regulatory subunits, the catalytic subunits are released and are thus free to catalyze the phosphorylation of an array of proteins, But cAMP fails to promote R subunit degradation by beta-catenin Bos taurus
additional information treatment of mitochondria with electron transport chain inhibitors rotenone, antimycin A, sodium azide, and oligomycin, as well as an uncoupler of oxidative phosphorylation, elicits enhanced C subunit activity. The catalytic subunit can exist in an inactive state via association with IkappaB in an NF-kappaB-IkappaB-(C subunit) complex. Stimulation of cells with lipopolysaccharide, endotheln-1, or angiotensin II induces IkappaB degradation, resulting in the ensuing C subunit-catalyzed phosphorylation of NF-kappaB p65 Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
additional information the C subunit is inactivated by Zn2+-metalloprotease-mediated proteolysis Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Bos taurus 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification regulatory subunits of the PKA holoenzyme, but not the catalytic subunits, suffer proteolysis, selectively in a calpain-dependent fashion, upon exposure of bovine heart mitochondria to digitonin, Ca2+, and a myriad of electron transport inhibitors. Attenuation of proteolysis in the presence of calpain inhibitor I. The C subunit is inactivated by Zn2+-metalloprotease-mediated proteolysis Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
heart
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + NF-kappaB p65 phosphorylation by the catalytic subunit of PKA Bos taurus ADP + phoshorylated NF-kappaB p65
-
 ?

Synonyms

Synonyms Comment Organism
PKA
-
 Bos taurus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Bos taurus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
 assay at Bos taurus

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Bos taurus

General Information

General Information Comment Organism
additional information mitochondrial cAMP-dependent protein kinase is activatable in a cAMP-independent fashion. Signals, originating from cAMP-independent sources, elicit enhanced mitochondrial PKA activity, overview Bos taurus