July 15, 2019Proceedings of the National Academy of SciencesOpen Access

Site-specific phosphorylation of myosin binding protein-C coordinates thin and thick filament activation in cardiac muscle

View Full Paper

Ask AI

Bookmark

Why the study?

Although phosphorylation of cMyBP-C is a recognized key regulator of myocardial contractility, little is known about its mechanism of action.

Structured PICO

Population

Isolated cardiac native thin filaments, the S2 domain of cardiac myosin, and intact heart muscle cells

Intervention

Site-specific phosphorylation of cardiac myosin binding protein-C (cMyBP-C) by protein kinases PKA, PKCε, and RSK2

Comparator

Different phosphorylation states or unphosphorylated states

Outcome

Protein-protein interactions with thin and thick filaments and structural changes in myofilamentssurrogate

Site-specific phosphorylation of cMyBP-C acts as a sarcomeric integrator of multiple signaling pathways to coordinate thin and thick filament activation in cardiac muscle.

Discussion

No takes yet. Share an insight, caveat, or question.

Implication

Does not support clinical changes in cardiac care; leaves open cMyBP-C phosphorylation as integrator of human sarcomeric signaling.

Cite This Study

Ponnam et al. (2019) studied this question.

synapsesocial.com/papers/69d8956652654bb436d19632 https://doi.org/10.1073/pnas.1903033116

View Full Paper

Ask AI

Bookmark

Site-specific phosphorylation of myosin binding protein-C coordinates thin and thick filament activation in cardiac muscle

Structured PICO

Discussion

Implication

Cite This Study

Site-specific phosphorylation of myosin binding protein-C coordinates thin and thick filament activation in cardiac muscle

Structured PICO

Discussion

Implication

Cite This Study

Also Consider

Also Consider