PRKACA phosphorylates PLN

Stable Identifier
Reaction [transition]
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
21108950 Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pump

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

J. Mol. Biol. 2011
22707725 Lethal, hereditary mutants of phospholamban elude phosphorylation by protein kinase A

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

J. Biol. Chem. 2012
Catalyst Activity

cAMP-dependent protein kinase activity of PRKACA [cytosol]

This event is regulated
Orthologous Events
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