What does this research mean for the field?

Phosphorylation of the M-domain reduces the functional potency of cardiac myosin-binding protein C (cMyBP-C) by compacting its structure, but this effect is antagonized and reversed by high calcium levels during peak contraction. Novelty: ClaimNovelty.NOVEL_FINDING. Consensus alignment: ConsensusAlignment.NEUTRAL.

February 23, 2016Proceedings of the National Academy of SciencesOpen Access

Phosphorylation and calcium antagonistically tune myosin-binding protein C’s structure and function

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Structured PICO

Population

Cardiac myosin-binding protein C (cMyBP-C) N-terminal domains (M-domain) and mutant proteins

Intervention

Phosphorylation of the M-domain and varying calcium levels

Comparator

Unphosphorylated state and low calcium levels

Outcome

M-domain extensibility, N-terminal domain conformation, and maximal sliding velocity in motility assayssurrogate

M-domain phosphorylation tunes cMyBP-C's calcium-sensitization primarily at low calcium levels between contractions, while peak calcium levels allow it to remain a potent contractile modulator regardless of phosphorylation state.

Discussion

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Implication

Animal data show calcium overrides phosphorylation effects on cMyBP-C; extends mechanistic insights but leaves human translation open.

Cite This Study

Previs et al. (2016) studied this question.

synapsesocial.com/papers/6a1be651ea84844e355f2615 https://doi.org/10.1073/pnas.1522236113

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Phosphorylation and calcium antagonistically tune myosin-binding protein C’s structure and function

Structured PICO

Discussion

Implication

Cite This Study

Phosphorylation and calcium antagonistically tune myosin-binding protein C’s structure and function

Structured PICO

Discussion

Implication

Cite This Study

Also Consider

Also Consider