Phosphoregulation of tropomyosin-actin interaction revealed using a genetic code expansion strategy.
Actin
Cytokineses
Synthetic biology
Tropomyosin
Journal
Wellcome open research
ISSN: 2398-502X
Titre abrégé: Wellcome Open Res
Pays: England
ID NLM: 101696457
Informations de publication
Date de publication:
2020
2020
Historique:
accepted:
03
07
2020
entrez:
18
8
2020
pubmed:
18
8
2020
medline:
18
8
2020
Statut:
epublish
Résumé
Tropomyosins are coiled-coil proteins that regulate the stability and / or function of actin cytoskeleton in muscle and non-muscle cells through direct binding of actin filaments. Recently, using the fission yeast, we discovered a new mechanism by which phosphorylation of serine 125 of tropomyosin (Cdc8), reduced its affinity for actin filaments thereby providing access for the actin severing protein Adf1/Cofilin to actin filaments causing instability of actin filaments. Here we use a genetic code expansion strategy to directly examine this conclusion. We produced in
Identifiants
pubmed: 32802966
doi: 10.12688/wellcomeopenres.16082.1
pmc: PMC7411518
doi:
Banques de données
figshare
['10.6084/m9.figshare.12490022.v1']
Types de publication
Journal Article
Langues
eng
Pagination
161Informations de copyright
Copyright: © 2020 Palani S et al.
Déclaration de conflit d'intérêts
No competing interests were disclosed.
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