The N terminus of myosin-binding protein C extends toward actin filaments in intact cardiac muscle
Myosin and actin filaments are highly organized within muscle sarcomeres. Myosin-binding protein C (MyBP-C) is a flexible, rod-like protein located within the C-zone of the sarcomere. The C-terminal domain of MyBP-C is tethered to the myosin filament backbone, and the N-terminal domains are postulat...
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Published in | The Journal of general physiology Vol. 153; no. 3; p. 1 |
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Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
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Rockefeller University Press
01.03.2021
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Abstract | Myosin and actin filaments are highly organized within muscle sarcomeres. Myosin-binding protein C (MyBP-C) is a flexible, rod-like protein located within the C-zone of the sarcomere. The C-terminal domain of MyBP-C is tethered to the myosin filament backbone, and the N-terminal domains are postulated to interact with actin and/or the myosin head to modulate filament sliding. To define where the N-terminal domains of MyBP-C are localized in the sarcomere of active and relaxed mouse myocardium, the relative positions of the N terminus of MyBP-C and actin were imaged in fixed muscle samples using super-resolution fluorescence microscopy. The resolution of the imaging was enhanced by particle averaging. The images demonstrate that the position of the N terminus of MyBP-C is biased toward the actin filaments in both active and relaxed muscle preparations. Comparison of the experimental images with images generated in silico, accounting for known binding partner interactions, suggests that the N-terminal domains of MyBP-C may bind to actin and possibly the myosin head but only when the myosin head is in the proximity of an actin filament. These physiologically relevant images help define the molecular mechanism by which the N-terminal domains of MyBP-C may search for, and capture, molecular binding partners to tune cardiac contractility. |
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AbstractList | Myosin and actin filaments are highly organized within muscle sarcomeres. Myosin-binding protein C (MyBP-C) is a flexible, rod-like protein located within the C-zone of the sarcomere. The C-terminal domain of MyBP-C is tethered to the myosin filament backbone, and the N-terminal domains are postulated to interact with actin and/or the myosin head to modulate filament sliding. To define where the N-terminal domains of MyBP-C are localized in the sarcomere of active and relaxed mouse myocardium, the relative positions of the N terminus of MyBP-C and actin were imaged in fixed muscle samples using super-resolution fluorescence microscopy. The resolution of the imaging was enhanced by particle averaging. The images demonstrate that the position of the N terminus of MyBP-C is biased toward the actin filaments in both active and relaxed muscle preparations. Comparison of the experimental images with images generated in silico, accounting for known binding partner interactions, suggests that the N-terminal domains of MyBP-C may bind to actin and possibly the myosin head but only when the myosin head is in the proximity of an actin filament. These physiologically relevant images help define the molecular mechanism by which the N-terminal domains of MyBP-C may search for, and capture, molecular binding partners to tune cardiac contractility. Myosin and actin filaments are highly organized within muscle sarcomeres. Myosin-binding protein C (MyBP-C) is a flexible, rod-like protein located within the C-zone of the sarcomere. The C-terminal domain of MyBP-C is tethered to the myosin filament backbone, and the N-terminal domains are postulated to interact with actin and/or the myosin head to modulate filament sliding. To define where the N-terminal domains of MyBP-C are localized in the sarcomere of active and relaxed mouse myocardium, the relative positions of the N terminus of MyBP-C and actin were imaged in fixed muscle samples using super-resolution fluorescence microscopy. The resolution of the imaging was enhanced by particle averaging. The images demonstrate that the position of the N terminus of MyBP-C is biased toward the actin filaments in both active and relaxed muscle preparations. Comparison of the experimental images with images generated in silico, accounting for known binding partner interactions, suggests that the N-terminal domains of MyBP-C may bind to actin and possibly the myosin head but only when the myosin head is in the proximity of an actin filament. These physiologically relevant images help define the molecular mechanism by which the N-terminal domains of MyBP-C may search for, and capture, molecular binding partners to tune cardiac contractility.Myosin and actin filaments are highly organized within muscle sarcomeres. Myosin-binding protein C (MyBP-C) is a flexible, rod-like protein located within the C-zone of the sarcomere. The C-terminal domain of MyBP-C is tethered to the myosin filament backbone, and the N-terminal domains are postulated to interact with actin and/or the myosin head to modulate filament sliding. To define where the N-terminal domains of MyBP-C are localized in the sarcomere of active and relaxed mouse myocardium, the relative positions of the N terminus of MyBP-C and actin were imaged in fixed muscle samples using super-resolution fluorescence microscopy. The resolution of the imaging was enhanced by particle averaging. The images demonstrate that the position of the N terminus of MyBP-C is biased toward the actin filaments in both active and relaxed muscle preparations. Comparison of the experimental images with images generated in silico, accounting for known binding partner interactions, suggests that the N-terminal domains of MyBP-C may bind to actin and possibly the myosin head but only when the myosin head is in the proximity of an actin filament. These physiologically relevant images help define the molecular mechanism by which the N-terminal domains of MyBP-C may search for, and capture, molecular binding partners to tune cardiac contractility. Using super-resolution fluorescence microscopy and in silico simulations, Rahmanseresht et al. demonstrate that the N terminus of myosin-binding protein C (MyBP-C) tends to bind to actin filaments in both active and relaxed muscle. Binding to the myosin head also appears possible but only when the myosin head is near the actin filament. Myosin and actin filaments are highly organized within muscle sarcomeres. Myosin-binding protein C (MyBP-C) is a flexible, rod-like protein located within the C-zone of the sarcomere. The C-terminal domain of MyBP-C is tethered to the myosin filament backbone, and the N-terminal domains are postulated to interact with actin and/or the myosin head to modulate filament sliding. To define where the N-terminal domains of MyBP-C are localized in the sarcomere of active and relaxed mouse myocardium, the relative positions of the N terminus of MyBP-C and actin were imaged in fixed muscle samples using super-resolution fluorescence microscopy. The resolution of the imaging was enhanced by particle averaging. The images demonstrate that the position of the N terminus of MyBP-C is biased toward the actin filaments in both active and relaxed muscle preparations. Comparison of the experimental images with images generated in silico, accounting for known binding partner interactions, suggests that the N-terminal domains of MyBP-C may bind to actin and possibly the myosin head but only when the myosin head is in the proximity of an actin filament. These physiologically relevant images help define the molecular mechanism by which the N-terminal domains of MyBP-C may search for, and capture, molecular binding partners to tune cardiac contractility. |
Author | Robbins, Jeffrey O'Leary, Thomas S Sadayappan, Sakthivel Previs, Michael J Warshaw, David M Lee, Kyoung H Craig, Roger Rahmanseresht, Sheema McNamara, James W |
AuthorAffiliation | 2 Division of Cell Biology and Imaging, Department of Radiology, University of Massachusetts Medical School, Worcester, MA 3 Heart, Lung and Vascular Institute, Department of Internal Medicine, Division of Cardiovascular Health and Disease, University of Cincinnati, Cincinnati, OH 1 Department of Molecular Physiology and Biophysics, Cardiovascular Research Institute, University of Vermont, Burlington, VT 4 Department of Pediatrics and the Heart Institute, Cincinnati Children’s Hospital Medical Center, Cincinnati, OH |
AuthorAffiliation_xml | – name: 2 Division of Cell Biology and Imaging, Department of Radiology, University of Massachusetts Medical School, Worcester, MA – name: 3 Heart, Lung and Vascular Institute, Department of Internal Medicine, Division of Cardiovascular Health and Disease, University of Cincinnati, Cincinnati, OH – name: 1 Department of Molecular Physiology and Biophysics, Cardiovascular Research Institute, University of Vermont, Burlington, VT – name: 4 Department of Pediatrics and the Heart Institute, Cincinnati Children’s Hospital Medical Center, Cincinnati, OH |
Author_xml | – sequence: 1 givenname: Sheema surname: Rahmanseresht fullname: Rahmanseresht, Sheema organization: Department of Molecular Physiology and Biophysics, Cardiovascular Research Institute, University of Vermont, Burlington, VT – sequence: 2 givenname: Kyoung H surname: Lee fullname: Lee, Kyoung H organization: Division of Cell Biology and Imaging, Department of Radiology, University of Massachusetts Medical School, Worcester, MA – sequence: 3 givenname: Thomas S surname: O'Leary fullname: O'Leary, Thomas S organization: Department of Molecular Physiology and Biophysics, Cardiovascular Research Institute, University of Vermont, Burlington, VT – sequence: 4 givenname: James W surname: McNamara fullname: McNamara, James W organization: Heart, Lung and Vascular Institute, Department of Internal Medicine, Division of Cardiovascular Health and Disease, University of Cincinnati, Cincinnati, OH – sequence: 5 givenname: Sakthivel surname: Sadayappan fullname: Sadayappan, Sakthivel organization: Heart, Lung and Vascular Institute, Department of Internal Medicine, Division of Cardiovascular Health and Disease, University of Cincinnati, Cincinnati, OH – sequence: 6 givenname: Jeffrey surname: Robbins fullname: Robbins, Jeffrey organization: Department of Pediatrics and the Heart Institute, Cincinnati Children's Hospital Medical Center, Cincinnati, OH – sequence: 7 givenname: David M surname: Warshaw fullname: Warshaw, David M organization: Department of Molecular Physiology and Biophysics, Cardiovascular Research Institute, University of Vermont, Burlington, VT – sequence: 8 givenname: Roger surname: Craig fullname: Craig, Roger organization: Division of Cell Biology and Imaging, Department of Radiology, University of Massachusetts Medical School, Worcester, MA – sequence: 9 givenname: Michael J surname: Previs fullname: Previs, Michael J organization: Department of Molecular Physiology and Biophysics, Cardiovascular Research Institute, University of Vermont, Burlington, VT |
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Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 J.W. McNamara’s present address is Murdoch Children’s Research Institute, The Royal Children’s Hospital, Parkville, Victoria, Australia. This work is part of a special collection on myofilament function and disease. S. Rahmanseresht and K.H. Lee contributed equally to this paper. K.H. Lee’s present address is Massachusetts Facility for High-Resolution Electron Cryo-microscopy, University of Massachusetts Medical School, Worcester, MA. |
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Snippet | Myosin and actin filaments are highly organized within muscle sarcomeres. Myosin-binding protein C (MyBP-C) is a flexible, rod-like protein located within the... Using super-resolution fluorescence microscopy and in silico simulations, Rahmanseresht et al. demonstrate that the N terminus of myosin-binding protein C... |
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SubjectTerms | Actin Actin Cytoskeleton - metabolism Animals Biophysics Cardiac muscle Carrier Proteins - metabolism Contraction and cell motility Filaments Fluorescence microscopy Mice Molecular physiology Muscle contraction Myocardium Myocardium - metabolism Myofilament Special Issue, 2020 Myosin Myosin-binding protein C Protein Binding Protein C Protein structure and dynamics Proteins Sarcomeres Sarcomeres - metabolism |
Title | The N terminus of myosin-binding protein C extends toward actin filaments in intact cardiac muscle |
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