Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Editorial
. 2016 Jul 1;111(1):5-7.
doi: 10.1093/cvr/cvw098. Epub 2016 May 17.

Myosin light chain phosphorylation, novel targets to repair a broken heart?

Danuta Szczesna-Cordary  1 , Pieter P de Tombe  2
Affiliations
Editorial

Myosin light chain phosphorylation, novel targets to repair a broken heart?

Danuta Szczesna-Cordary et al. Cardiovasc Res. .
No abstract available

PubMed Disclaimer

Figures

Figure 1
Figure 1
Cardiac myosin light chains in health and disease. The cardiac sarcomere contains myosin located in the thick filament and actin located in the thin filament (A). Cardiac muscle contraction is controlled by access of the myosin heads to actin binding sites on the thin filament. This process starts with the binding of calcium to troponin (positioned on the thin filament), which causes a structural repositioning of the coiled-coil tropomyosin molecule within the grooves of the double-stranded actin filament, thereby exposing actin-binding sites on the thin filament for the myosin heads to bind and develop contractile force. Moreover, it has been suggested that the N-terminus of the ELC may interact with thin-filament actin and functionally modulate thin-filament regulation and muscle contraction (A). Each myosin head is composed of the myosin heavy chain (MHC; cyan), one regulatory light chain (RLC; red), and one essential light chain (ELC; green) (B). Both myosin light chains can be phosphorylated at ELC-Ser195 and RLC-Ser-15 (C), and this process has been postulated to play a role in the normal function of the heart. Diminished phosphorylation of either light chain may negatively impact cardiac function, particularly under conditions of haemodynamic stress (C). Modulation of the light chain phosphorylation (RLC and/or ELC) may provide a pathway for the development of novel treatment strategies to combat heart failure, an entity of ever increasing clinical significance.
See this image and copyright information in PMC

Comment on

References

    1. Geeves MA, Holmes KC. The molecular mechanism of muscle contraction. Adv Protein Chem 2005;71:161–193. - PubMed
    1. Rayment I, Rypniewski WR, Schmidt-Base K, Smith R, Tomchick DR, Benning MM et al. . Three-dimensional structure of myosin subfragment-1: a molecular motor. Science 1993;261:50–58. - PubMed
    1. Arrell DK, Neverova I, Fraser H, Marban E, Van Eyk JE. Proteomic analysis of pharmacologically preconditioned cardiomyocytes reveals novel phosphorylation of myosin light chain 1. Circ Res 2001;89:480–487. - PubMed
    1. Massengill MT, Ashraf HM, Chowdhury RR, Chrzanowski SM, Kar J, Warren SA et al. . Acute heart failure with cardiomyocyte atrophy induced in adult mice by ablation of cardiac myosin light chain kinase. Cardiovasc Res 2016;111:34–43. - PMC - PubMed
    1. Scheid LM, Mosqueira M, Hein S, Kossack M, Juergensen L, Mueller M et al. . Essential light chain S195 phosphorylation is required for cardiac adaptation under physical stress. Cardiovasc Res 2016;111:44–55. - PubMed

LinkOut - more resources