Cardiac myosin binding protein-C phosphorylation accelerates β-cardiac myosin detachment rate in mouse myocardium-Reference-Cited by-同舟云学术

Cardiac myosin binding protein-C phosphorylation accelerates β-cardiac myosin detachment rate in mouse myocardium

Published:2021-05-01 Issue:5 Volume:320 Page:H1822-H1835
ISSN:0363-6135
Container-title:American Journal of Physiology-Heart and Circulatory Physiology
language:en
Short-container-title:American Journal of Physiology-Heart and Circulatory Physiology

Author:

Tanner Bertrand C. W.¹^ORCID,Previs Michael J.¹^ORCID,Wang Yuan¹,Robbins Jeffrey²,Palmer Bradley M.¹

Affiliation:

1. Department of Molecular Physiology and Biophysics, University of Vermont, Burlington, Vermont

2. Department of Pediatrics, Cincinnati Children’s Hospital Medical Center, Cincinnati, Ohio

Abstract

Length perturbation analysis was used to demonstrate that β-cardiac myosin characteristic rates of detachment and recruitment in the intact myofilament lattice are accelerated by Pi, phosphorylation of cMyBP-C, and the absence of cMyBP-C. The results suggest that cMyBP-C normally slows myosin detachment, including Pi-dependent detachment, and that this inhibition is released with phosphorylation or absence of cMyBP-C.

Funder

HHS | NIH | National Heart, Lung, and Blood Institute

Publisher

American Physiological Society

Subject

Physiology (medical),Cardiology and Cardiovascular Medicine,Physiology

Link

https://journals.physiology.org/doi/pdf/10.1152/ajpheart.00673.2020

Reference55 articles.

1. Determination of the critical residues responsible for cardiac myosin binding protein C's interactions

2. Effects of the N-terminal Domains of Myosin Binding Protein-C in an in Vitro Motility Assay

3. Structural Evidence for the Interaction of C-protein (MyBP-C) with Actin and Sequence Identification of a Possible Actin-binding Domain