PRKACA phosphorylates TNNI3

Stable Identifier
R-HSA-5617179
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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Human cardiac troponin I (TNNI3) is known to be phosphorylated at multiple amino acid residue sites by several kinases. Protein kinase A (PRKACA) can phosphorylate serine 23 and 24 sites on TNNI3. Phosphorylation of TNNI3 reduces myofilament calcium sensitivity (Mittmann et al. 1990, Keane et al. 1997, Zhang et al. 2012). Defects in TNNI3 can cause a range of cardiomyopathies (Lu et al. 2013). 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
2226863 A common motif of two adjacent phosphoserines in bovine, rabbit and human cardiac troponin I

Mittmann, K, Jaquet, K, Heilmeyer, LM

FEBS Lett. 1990
23610579 Inherited cardiomyopathies caused by troponin mutations

Lu, QW, Wu, XY, Morimoto, S

J Geriatr Cardiol 2013
22972900 Multiple reaction monitoring to identify site-specific troponin I phosphorylated residues in the failing human heart

Zhang, P, Kirk, JA, Ji, W, dos Remedios, CG, Kass, DA, Van Eyk, JE, Murphy, AM

Circulation 2012
9346285 The ordered phosphorylation of cardiac troponin I by the cAMP-dependent protein kinase--structural consequences and functional implications

Keane, NE, Quirk, PG, Gao, Y, Patchell, VB, Perry, SV, Levine, BA

Eur. J. Biochem. 1997
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hasEvent
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Catalyst Activity
Title
cAMP-dependent protein kinase activity of PRKACA [cytosol]
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This event is regulated
Orthologous Events
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