ArticleJournal of molecular biology2011
The N-terminal domains of myosin binding protein C can bind polymorphically to F-actin.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
40 citing papers in PubMed, 54 citations in OpenAlex.
- The D75N and P161S Mutations in the C0-C2 Fragment of cMyBP-C Associated with Hypertrophic Cardiomyopathy Disturb the Thin Filament Activation, Nucleotide Exchange in Myosin, and Actin-Myosin Interaction.International journal of molecular sciences · 2024Article
- Bringing into focus the central domains C3-C6 of myosin binding protein C.Frontiers in physiology · 2024Review
- Interaction of the C2 Ig-like Domain of Cardiac Myosin Binding Protein-C with F-actin.Journal of molecular biology · 2021Article
- A high-throughput fluorescence lifetime-based assay to detect binding of myosin-binding protein C to F-actin.The Journal of general physiology · 2021Article
- MyBP-C: one protein to govern them all.Journal of muscle research and cell motility · 2020Review
- Human cardiac myosin-binding protein C restricts actin structural dynamics in a cooperative and phosphorylation-sensitive manner.The Journal of biological chemistry · 2019Article
- Revealing the mechanism of how cardiac myosin-binding protein C N-terminal fragments sensitize thin filaments for myosin binding.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Role of intrinsic disorder in muscle sarcomeres.Progress in molecular biology and translational science · 2019Review
- N-Terminal Domains of Cardiac Myosin Binding Protein C Cooperatively Activate the Thin Filament.Structure (London, England : 1993) · 2018Article
- Point mutations in the tri-helix bundle of the M-domain of cardiac myosin binding protein-C influence systolic duration and delay cardiac relaxation.Journal of molecular and cellular cardiology · 2018Article
- Thick Filament Protein Network, Functions, and Disease Association.Comprehensive Physiology · 2018Review
- Phosphorylation of cardiac myosin binding protein C releases myosin heads from the surface of cardiac thick filaments.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- In vivo definition of cardiac myosin-binding protein C's critical interactions with myosin.Pflugers Archiv : European journal of physiology · 2016Article
- Slowing of contractile kinetics by myosin-binding protein C can be explained by its cooperative binding to the thin filament.Journal of molecular and cellular cardiology · 2016Article
- The A31P missense mutation in cardiac myosin binding protein C alters protein structure but does not cause haploinsufficiency.Archives of biochemistry and biophysics · 2016Article
- C0 and C1 N-terminal Ig domains of myosin binding protein C exert different effects on thin filament activation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The cMyBP-C HCM variant L348P enhances thin filament activation through an increased shift in tropomyosin position.Journal of molecular and cellular cardiology · 2016Article
- MYBPC1, an Emerging Myopathic Gene: What We Know and What We Need to Learn.Frontiers in physiology · 2016Review
- Historical perspective on heart function: the Frank-Starling Law.Biophysical reviews · 2015Review
- Normal cardiac contraction in mice lacking the proline-alanine rich region and C1 domain of cardiac myosin binding protein C.Journal of molecular and cellular cardiology · 2015Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The regulation of vertebrate striated muscle contraction involves a number of different molecules, including the thin-filament accessory proteins tropomyosin and troponin that provide Ca(2+)-dependent regulation by controlling access to myosin binding sites on actin. Cardiac myosin binding protein C (cMyBP-C) appears to modulate this Ca(2+)-dependent regulation and has attracted increasing interest due to links with inherited cardiac diseases. A number of single amino acid mutations linked to clinical diseases occur in the N-terminal region of cMyBP-C, including domains C0 and C1, which previously have been shown to bind to F-actin. This N-terminal region also has been shown to both inhibit and activate actomyosin interactions in vitro. Using electron microscopy and three-dimensional reconstruction, we show that C0 and C1 can each bind to the same two distinctly different positions on F-actin. One position aligns well with the previously reported binding site that clashes with the binding of myosin to actin, but would force tropomyosin into an "on" position that exposes myosin binding sites along the filament. The second position identified here would not interfere with either myosin binding or tropomyosin positioning. It thus appears that the ability to bind to at least two distinctly different positions on F-actin, as observed for tropomyosin, may be more common than previously considered for other actin binding proteins. These observations help to explain many of the seemingly contradictory results obtained with cMyBP-C and show how cMyBP-C can provide an additional layer of regulation to actin-myosin interactions. They also suggest a redundancy of C0 and C1 that may explain the absence of C0 in skeletal muscle.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.