Phosphorylated cofilin-2 is more prone to oxidative modifications on Cys39 and favors amyloid fibril formation.
Amyloid
Cofilin
Cysteine
Phosphorylation
Redox properties
Sulfide
Journal
Redox biology
ISSN: 2213-2317
Titre abrégé: Redox Biol
Pays: Netherlands
ID NLM: 101605639
Informations de publication
Date de publication:
10 2020
10 2020
Historique:
received:
24
05
2020
revised:
06
08
2020
accepted:
17
08
2020
pubmed:
31
8
2020
medline:
22
6
2021
entrez:
1
9
2020
Statut:
ppublish
Résumé
Cofilins are small protein of the actin depolymerizing family. Actin polymerization/depolymerization is central to a number of critical cellular physiological tasks making cofilin a key protein for several physiological functions of the cell. Cofilin activity is mainly regulated by phosphorylation on serine residue 3 making this post-translational modification key to the regulation of myofilament integrity. In fact, in this form, the protein segregates in myocardial aggregates in human idiopathic dilated cardiomyopathy. Since myofilament network is an early target of oxidative stress we investigated the molecular changes induced by oxidation on cofilin isoforms and their interplay with the protein phosphorylation state to get insight on whether/how those changes may predispose to early protein aggregation. Using different and complementary approaches we characterized the aggregation properties of cofilin-2 and its phosphomimetic variant (S3D) in response to oxidative stress in silico, in vitro and on isolated cardiomyocytes. We found that the phosphorylated (inactive) form of cofilin-2 is mechanistically linked to the formation of an extended network of fibrillar structures induced by oxidative stress via the formation of a disulfide bond between Cys39 and Cys80. Such phosphorylation-dependent effect is likely controlled by changes in the hydrogen bonding network involving Cys39. We found that the sulfide ion inhibits the formation of such structures. This might represent the mechanism for the protective effect of the therapeutic agent Na
Identifiants
pubmed: 32863228
pii: S2213-2317(20)30896-X
doi: 10.1016/j.redox.2020.101691
pmc: PMC7472925
pii:
doi:
Substances chimiques
Actin Depolymerizing Factors
0
Actins
0
Amyloid
0
CFL2 protein, human
0
Cofilin 2
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
101691Informations de copyright
Copyright © 2020 The Author(s). Published by Elsevier B.V. All rights reserved.
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