The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies - Sorbonne Université Access content directly
Journal Articles Cell Reports Year : 2021

The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies

Hugo Wioland
Alain Schmitt
  • Function : Author
Wei Wu
Antoine Jégou

Abstract

Cofilins are important for the regulation of the actin cytoskeleton, sarcomere organization, and force production. The role of cofilin-1, the non-muscle-specific isoform, in muscle function remains unclear. Mutations in LMNA encoding A-type lamins, intermediate filament proteins of the nuclear envelope, cause autosomal Emery-Dreifuss muscular dystrophy (EDMD). Here, we report increased cofilin-1 expression in LMNA mutant muscle cells caused by the inability of proteasome degradation, suggesting a protective role by ERK1/2. It is known that phosphorylated ERK1/2 directly binds to and catalyzes phosphorylation of the actin-depolymerizing factor cofilin-1 on Thr25. In vivo ectopic expression of cofilin-1, as well as its phosphorylated form on Thr25, impairs sarcomere structure and force generation. These findings present a mechanism that provides insight into the molecular pathogenesis of muscular dystrophies caused by LMNA mutations.
Fichier principal
Vignette du fichier
1-s2.0-S2211124721010391-main.pdf (5.21 Mo) Télécharger le fichier
Origin Publication funded by an institution

Dates and versions

hal-03350074 , version 1 (21-09-2021)

Identifiers

Cite

Nicolas Vignier, Maria Chatzifrangkeskou, Luca Pinton, Hugo Wioland, Thibaut Marais, et al.. The non-muscle ADF/cofilin-1 controls sarcomeric actin filament integrity and force production in striated muscle laminopathies. Cell Reports, 2021, 36 (8), pp.109601. ⟨10.1016/j.celrep.2021.109601⟩. ⟨hal-03350074⟩
99 View
28 Download

Altmetric

Share

Gmail Mastodon Facebook X LinkedIn More