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January 13, 2004Circulation Research

Protein Kinase A Phosphorylation at Serine-2808 of the Cardiac Ca 2+ -Release Channel (Ryanodine Receptor) Does Not Dissociate 12.6-kDa FK506-Binding Protein (FKBP12.6)

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Population

Recombinant or native FKBP12.6-RyR2 complex

Comparison

PKA phosphorylation and mutations at serine-2808… vs Nonphosphorylated form of RyR2

Design

Preclinical

Key result

Complete phosphorylation at serine-2808 of RyR2 by exogenous PKA did not disrupt the recombinant or native FKBP12.6-RyR2 complex.

Authors

BXBailong XiaoCSCindy SutherlandMWMichael P. Walsh

Discussion

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Overview

Basic science data on RyR2-FKBP12.6 dissociation warrant no clinical change in HF; leaves open mechanistic role of S2808 phosphorylation.

Structured PICO

P
Population
Recombinant or native FKBP12.6-RyR2 complex
I
Intervention
PKA phosphorylation and mutations (S2808D) at serine-2808 of RyR2
C
Comparator
Nonphosphorylated form of RyR2
O
Outcome
Dissociation of FKBP12.6 from RyR2surrogate

PKA phosphorylation at serine-2808 of RyR2 does not dissociate FKBP12.6, challenging a previously proposed mechanism for cardiac dysfunction in heart failure.

Cite This Study

Xiao et al. (2004) studied this question. PKA phosphorylation at serine-2808 of RyR2 vs. Nonphosphorylated RyR2 was evaluated on Dissociation of FKBP12.6 from RyR2. Complete phosphorylation at serine-2808 of RyR2 by exogenous PKA did not disrupt the recombinant or native FKBP12.6-RyR2 complex.

synapsesocial.com/papers/6a63aa1ba8b6909d49095db1https://doi.org/10.1161/01.res.0000115945.89741.22
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