Troponin and a Myopathy-Linked Mutation in
actin
cofilin-2
myopathy
thin filament
tropomyosin
troponin
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
17 Nov 2023
17 Nov 2023
Historique:
received:
18
10
2023
revised:
10
11
2023
accepted:
13
11
2023
medline:
27
11
2023
pubmed:
25
11
2023
entrez:
25
11
2023
Statut:
epublish
Résumé
Uniform actin filament length is required for synchronized contraction of skeletal muscle. In myopathies linked to mutations in tropomyosin (Tpm) genes, irregular thin filaments are a common feature, which may result from defects in length maintenance mechanisms. The current work investigated the effects of the myopathy-causing p.R91C variant in Tpm3.12, a tropomyosin isoform expressed in slow-twitch muscle fibers, on the regulation of actin severing and depolymerization by cofilin-2. The affinity of cofilin-2 for F-actin was not significantly changed by either Tpm3.12 or Tpm3.12-R91C, though it increased two-fold in the presence of troponin (without Ca
Identifiants
pubmed: 38003645
pii: ijms242216457
doi: 10.3390/ijms242216457
pmc: PMC10671271
pii:
doi:
Substances chimiques
Actins
0
Cofilin 2
0
TPM3 protein, human
0
Tropomyosin
0
Troponin
0
CFL2 protein, human
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : Polish Minister of Education and Science under the program Regional Initiative of Excellence in 2019-2023
ID : 008/RID/2018/19
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