Cardiomyopathic mutations in essential light chain reveal mechanisms regulating the super relaxed state of myosin.


Journal

The Journal of general physiology
ISSN: 1540-7748
Titre abrégé: J Gen Physiol
Pays: United States
ID NLM: 2985110R

Informations de publication

Date de publication:
05 07 2021
Historique:
received: 19 10 2020
revised: 06 04 2021
accepted: 27 04 2021
entrez: 20 5 2021
pubmed: 21 5 2021
medline: 16 10 2021
Statut: ppublish

Résumé

In this study, we assessed the super relaxed (SRX) state of myosin and sarcomeric protein phosphorylation in two pathological models of cardiomyopathy and in a near-physiological model of cardiac hypertrophy. The cardiomyopathy models differ in disease progression and severity and express the hypertrophic (HCM-A57G) or restrictive (RCM-E143K) mutations in the human ventricular myosin essential light chain (ELC), which is encoded by the MYL3 gene. Their effects were compared with near-physiological heart remodeling, represented by the N-terminally truncated ELC (Δ43 ELC mice), and with nonmutated human ventricular WT-ELC mice. The HCM-A57G and RCM-E143K mutations had antagonistic effects on the ATP-dependent myosin energetic states, with HCM-A57G cross-bridges fostering the disordered relaxed (DRX) state and the RCM-E143K model favoring the energy-conserving SRX state. The HCM-A57G model promoted the switch from the SRX to DRX state and showed an ∼40% increase in myosin regulatory light chain (RLC) phosphorylation compared with the RLC of normal WT-ELC myocardium. On the contrary, the RCM-E143K-associated stabilization of the SRX state was accompanied by an approximately twofold lower level of myosin RLC phosphorylation compared with the RLC of WT-ELC. Upregulation of RLC phosphorylation was also observed in Δ43 versus WT-ELC hearts, and the Δ43 myosin favored the energy-saving SRX conformation. The two disease variants also differently affected the duration of force transients, with shorter (HCM-A57G) or longer (RCM-E143K) transients measured in electrically stimulated papillary muscles from these pathological models, while no changes were displayed by Δ43 fibers. We propose that the N terminus of ELC (N-ELC), which is missing in the hearts of Δ43 mice, works as an energetic switch promoting the SRX-to-DRX transition and contributing to the regulation of myosin RLC phosphorylation in full-length ELC mice by facilitating or sterically blocking RLC phosphorylation in HCM-A57G and RCM-E143K hearts, respectively.

Identifiants

pubmed: 34014247
pii: 212172
doi: 10.1085/jgp.202012801
pmc: PMC8142263
pii:
doi:

Substances chimiques

Myosin Light Chains 0

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Subventions

Organisme : NHLBI NIH HHS
ID : R01 HL143830
Pays : United States
Organisme : NHLBI NIH HHS
ID : R56 HL146133
Pays : United States

Informations de copyright

© 2021 Sitbon et al.

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Auteurs

Yoel H Sitbon (YH)

Department of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, FL.

Francisca Diaz (F)

Department of Neurology, University of Miami Miller School of Medicine, Miami, FL.

Katarzyna Kazmierczak (K)

Department of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, FL.

Jingsheng Liang (J)

Department of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, FL.

Medhi Wangpaichitr (M)

VA Health Care System, Research Service, Miami, FL.

Danuta Szczesna-Cordary (D)

Department of Molecular and Cellular Pharmacology, University of Miami Miller School of Medicine, Miami, FL.

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