Protein arginylation of cytoskeletal proteins in the muscle: modifications modifying function.
actin
arginylation
muscle
myosin
posttranslational modification
Journal
American journal of physiology. Cell physiology
ISSN: 1522-1563
Titre abrégé: Am J Physiol Cell Physiol
Pays: United States
ID NLM: 100901225
Informations de publication
Date de publication:
01 05 2019
01 05 2019
Historique:
pubmed:
23
2
2019
medline:
14
2
2020
entrez:
22
2
2019
Statut:
ppublish
Résumé
The cytoskeleton drives many essential processes in normal physiology, and its impairments underlie many diseases, including skeletal myopathies, cancer, and heart failure, that broadly affect developed countries worldwide. Cytoskeleton regulation is a field of investigation of rapidly emerging global importance and a new venue for the development of potential therapies. This review overviews our present understanding of the posttranslational regulation of the muscle cytoskeleton through arginylation, a tRNA-dependent addition of arginine to proteins mediated by arginyltransferase 1. We focus largely on arginylation-dependent regulation of striated muscles, shown to play critical roles in facilitating muscle integrity, contractility, regulation, and strength.
Identifiants
pubmed: 30789755
doi: 10.1152/ajpcell.00500.2018
pmc: PMC6580163
doi:
Substances chimiques
Cytoskeletal Proteins
0
Arginine
94ZLA3W45F
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
C668-C677Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM122505
Pays : United States
Organisme : CIHR
ID : 125898
Pays : Canada
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