What is the clinical evidence from this study?

Intervention: PKA-mediated phosphorylation of C0-C2. Primary outcome: Actin structural dynamics.

What does this research mean for the field?

PKA-mediated phosphorylation of the C0-C2 domains of cardiac myosin-binding protein C eliminates cooperative effects on actin flexibility and increases actin rotational rates, modulating actin dynamics to influence actin-myosin interactions. Novelty: ClaimNovelty.INCREMENTAL. Consensus alignment: ConsensusAlignment.NEUTRAL.

September 13, 2019Journal of Biological ChemistryOpen Access

Human cardiac myosin–binding protein C restricts actin structural dynamics in a cooperative and phosphorylation-sensitive manner

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Key result

PKA-mediated phosphorylation of cMyBP-C C0-C2 domains eliminated cooperative effects on actin flexibility and modestly increased actin rotational rates.

Comparison

Phosphorylation and phosphomimetic substitutions vs unphosphorylated C0-C2 or C0-C1

Design

In vitro experimental study

Authors

TBThomas A. BunchUniversity of Arizona RKRhye‐Samuel KanassategaUniversity of Arizona VLVictoria C. LepakHeart Failure / Cardiomyopathy

Discussion

Member takes

Implication

These actin dynamics in animal models warrant targeted follow-up; leaves open relevance to human cardiac therapies.

Structured PICO

Population

in vitro model studying human cardiac myosin-binding protein C (cMyBP-C) and actin structural dynamics

Intervention

PKA-mediated phosphorylation of C0-C2 and phosphomimetic substitutions

Comparator

unphosphorylated state or C0-C1 (lacking M-domain/C2)

Outcome

actin structural dynamics (flexibility and rotational rates)

cMyBP-C binding and PKA-mediated phosphorylation modulate actin dynamics, providing a mechanistic explanation for the functional effects of cMyBP-C phosphorylation on actin-myosin interactions.

Cite This Study

Bunch et al. (2019) studied this question. PKA-mediated phosphorylation of C0-C2 was evaluated on Actin structural dynamics. PKA-mediated phosphorylation of cMyBP-C C0-C2 domains eliminated cooperative effects on actin flexibility and modestly increased actin rotational rates.

synapsesocial.com/papers/6a15cc9c814bf8ec9a4f0e8f https://doi.org/10.1074/jbc.ra119.009543

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Human cardiac myosin–binding protein C restricts actin structural dynamics in a cooperative and phosphorylation-sensitive manner

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Human cardiac myosin–binding protein C restricts actin structural dynamics in a cooperative and phosphorylation-sensitive manner

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider