Phosphorylation-dependent interactions of myosin-binding protein C and troponin coordinate the myofilament response to protein kinase A.

Calcium / metabolism Cyclic AMP-Dependent Protein Kinases / metabolism Myocardium / metabolism Myofibrils / metabolism Phosphorylation Troponin I / metabolism Carrier Proteins / metabolism
PKA cardiac troponin length-dependent activation myosin-binding protein C phosphorylation

Journal

The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R

Informations de publication

Date de publication:
01 2023
Historique:
received: 23 06 2022
revised: 23 11 2022
accepted: 24 11 2022
pubmed: 6 12 2022
medline: 28 1 2023
entrez: 5 12 2022
Statut: ppublish

Résumé

PKA-mediated phosphorylation of sarcomeric proteins enhances heart muscle performance in response to β-adrenergic stimulation and is associated with accelerated relaxation and increased cardiac output for a given preload. At the cellular level, the latter translates to a greater dependence of Ca

Identifiants

DOI: 10.1016/j.jbc.2022.102767 PMID: 36470422 PMC: PMC9826837
pubmed: 36470422
pii: S0021-9258(22)01210-8
doi: 10.1016/j.jbc.2022.102767
pmc: PMC9826837
pii:
doi:

Substances chimiques

Calcium SY7Q814VUP
Cyclic AMP-Dependent Protein Kinases EC 2.7.11.11
myosin-binding protein C 0
Troponin I 0
Carrier Proteins 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

102767

Subventions

Organisme : British Heart Foundation
ID : PG/16/19/32072
Pays : United Kingdom

Informations de copyright

Copyright © 2022 The Authors. Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Conflict of interests The authors declare that they have no conflicts of interest with the contents of this article.

Auteurs

Ivanka R Sevrieva (IR)

Randall Centre for Cell and Molecular Biophysics, and British Heart Foundation Centre of Research Excellence, King's College London, London, United Kingdom. Electronic address: ivanka.r.sevrieva@kcl.ac.uk.

Saraswathi Ponnam (S)

Randall Centre for Cell and Molecular Biophysics, and British Heart Foundation Centre of Research Excellence, King's College London, London, United Kingdom.

Ziqian Yan (Z)

Randall Centre for Cell and Molecular Biophysics, and British Heart Foundation Centre of Research Excellence, King's College London, London, United Kingdom.

Malcolm Irving (M)

Randall Centre for Cell and Molecular Biophysics, and British Heart Foundation Centre of Research Excellence, King's College London, London, United Kingdom.

Thomas Kampourakis (T)

Randall Centre for Cell and Molecular Biophysics, and British Heart Foundation Centre of Research Excellence, King's College London, London, United Kingdom.

Yin-Biao Sun (YB)

Randall Centre for Cell and Molecular Biophysics, and British Heart Foundation Centre of Research Excellence, King's College London, London, United Kingdom.

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Classifications MeSH

questionsmedicales.fr › Facteurs biologiques › Facteurs de la coagulation sanguine › Calcium › Phosphorylation-dependent interactions of...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protein-Serine-Threonine Kinases › Cyclic Nucleotide-Regulated Protein Kinases › Cyclic AMP-Dependent Protein Kinases › Phosphorylation-dependent interactions of...
questionsmedicales.fr › Tissus › Muscles › Muscle strié › Myocarde › Phosphorylation-dependent interactions of...
questionsmedicales.fr › Cellules › Cellules musculaires › Myocytes cardiaques › Myofibrilles › Phosphorylation-dependent interactions of...
questionsmedicales.fr › Métabolisme › Phosphorylation › Phosphorylation-dependent interactions of...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines du cytosquelette › Protéines des microfilaments › Troponine › Troponine I › Phosphorylation-dependent interactions of...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines de transport › Phosphorylation-dependent interactions of...