Expression of SUMO enzymes is fiber type dependent in skeletal muscles and is dysregulated in muscle disuse.
FASEB J
; 34(2): 2269-2286, 2020 02.
Article
en En
| MEDLINE
| ID: mdl-31908008
ABSTRACT
SUMOylation is a dynamic, reversible, enzymatic drug-targetable post-translational modification (PTM) reaction where the Small Ubiquitin-like Modifier (SUMO) moieties are attached to proteins. This reaction regulates various biological functions like cell growth, differentiation, and it is crucial for maintaining organ homeostasis. However, the actions of SUMO in skeletal muscle pathophysiology are still not investigated. In this study, we quantified the abundance of the SUMO enzymes and determined the distribution of SUMOylated proteins along the fibers of nine different muscles. We find that skeletal muscles contain a distinctive group of SUMO enzymes and SUMOylated proteins in relation to their different metabolism, functions, and fiber type composition. In addition, before the activation of protein degradation pathways, this unique set is quickly altered in response to muscle sedentariness. Finally, we demonstrated that PAX6 acts as an upstream regulator of the SUMO conjugation reaction, which can become a potential therapeutic marker to prevent muscle diseases generated by inactivity.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Atrofia Muscular
/
Músculo Esquelético
/
Proteínas Modificadoras Pequeñas Relacionadas con Ubiquitina
/
Enzimas Ubiquitina-Conjugadoras
/
Sumoilación
Límite:
Animals
Idioma:
En
Revista:
FASEB J
Asunto de la revista:
BIOLOGIA
/
FISIOLOGIA
Año:
2020
Tipo del documento:
Article
País de afiliación:
Suecia