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PRKAR2B — RYR2
Protein-Protein interactions - manually collected from original source literature:
Studies that report less than 10 interactions are marked with *
Text-mined interactions from Literome
Li et al., Circ Res 2002
(Calcium Signaling) :
However, clear cellular data on PKA dependent modulation of cardiac RyRs is limited because of difficulty in distinguishing between
PKA effects on
RyR , phospholamban (PLB), and Ca2+ current
Ruehr et al., J Biol Chem 2003
:
Therefore, localization of
PKA by mAKAP at RyR1
increases both PKA dependent RyR phosphorylation as well as efflux of Ca2+ through the
RyR
Lehnart et al., Curr Top Med Chem 2003
(Ion Channel Gating) :
In addition, the
FKBP-RyR interaction is
regulated by
PKA phosphorylation
Lehnart et al., Biochem Biophys Res Commun 2004
(Arrhythmias, Cardiac...) :
Calstabin2 binding to
RyR2 is
regulated by
PKA phosphorylation of Ser2809 in RyR2
Xiao et al., J Biol Chem 2007
:
Importantly, the S2030A mutation, but not mutations of Ser-2,808, diminished the
effect of
PKA on
RyR2
Jones et al., Biochem J 2008
:
To gain insight into the structural basis of the
regulation of
RyR2 by
PKA , we determined the three-dimensional location of the PKA site Ser2030
Morimoto et al., Biochem Biophys Res Commun 2009
:
The Ca ( 2+ ) leak in isoproterenol treated preparations was significantly increased when the
PKA dependent phosphorylation of
RyR was increased without the involvement of CaMKII dependent phosphorylation ... Both the increase in Ca ( 2+ ) leak and the phosphorylation of
RyR were
blocked by a
PKA inhibitor ... Our results show that beta-adrenergic stimulation increases Ca ( 2+ ) leak from SR through
PKA dependent phosphorylation of
RyR
Guo et al., Circ Res 2010
(Calcium Signaling) :
PKA dependent
RyR2 phosphorylation has no significant effect on binding of either FKBP12 or 12.6 to RyR2 in myocytes
Ullrich et al., J Mol Cell Cardiol 2012
:
During physical exercise and stress, the sympathetic system stimulates cardiac contractility via ß-adrenergic receptor activation, resulting in
protein kinase A (PKA) mediated phosphorylation of the cardiac
ryanodine receptor , RyR2, at Ser2808 ... We show here by three independent experimental approaches that
PKA dependent
RyR2-S2808 phosphorylation plays significant functional roles at the subcellular level, namely, Ca ( 2+ ) release synchronization, Ca ( 2+ ) wave propagation and functional adaptation of RyR2 to variable [ Ca ( 2+ ) ] ( SR )