PRKACA phosphorylates PLN

Stable Identifier
R-HSA-5617182
Type
Reaction [transition]
Species
Homo sapiens
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Cardiac muscle phospholamban (PLN aka PLB) modulates cardiac contractility by inhibiting the sarcoplasmic reticulum calcium pump (ATP2A2 aka SERCA). This process is dynamically regulated by beta-adrenergic stimulation and phosphorylation of PLN. Protein kinase A (PRKACA) is able to phosphorylate PLN at serine 16, relieving its inhibition of ATP2A2 and modulating cardiac contractility (Glaves et al. 2011, Ceholski et al. 2012). The ATP2B4:NOS1 complex, via cAMP, increases PRKACA activity, thereby regulating the response of the heart to beta-adrenergic agonists.

Literature References
PubMed ID Title Journal Year
22707725 Lethal, hereditary mutants of phospholamban elude phosphorylation by protein kinase A

Ceholski, DK, Trieber, CA, Holmes, CF, Young, HS

J. Biol. Chem. 2012
21108950 Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pump

Glaves, JP, Trieber, CA, Ceholski, DK, Stokes, DL, Young, HS

J. Mol. Biol. 2011
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hasEvent
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Catalyst Activity
Title
cAMP-dependent protein kinase activity of PRKACA [cytosol]
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