Glutathionylation of beta-actin via a cysteinyl sulfenic acid intermediary
Open Access
- 1 January 2007
- journal article
- Published by Springer Nature in BMC Biochemistry
- Vol. 8 (1) , 26
- https://doi.org/10.1186/1471-2091-8-26
Abstract
Cysteinyl residues in actin are glutathionylated, ie. form a mixed disulfide with glutathione, even in the absence of exogenous oxidative stress. Glutathionylation inhibits actin polymerization and reversible actin glutathionylation is a redox dependent mechanism for regulation of the cytoskeleton structure. The molecular mechanism that mediates actin glutathionylation in vivo is unclear.Keywords
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