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Updated: Sep 6, 2025

Author Spotlight: Microscopic Analysis of Protein Localization at Plasmodesmata in Plants
Published on: November 1, 2024
Thiol-disulfide oxidoreductase PDI1;1 regulates actin structures in Oryza sativa root cells
1Graduate School of Agriculture, Ehime University, Matsuyama, Japan.
Abstract:
The polarized and dynamic actin cytoskeleton is essential for root cell growth. Here, we report the key role of thiol-disulfide oxidoreductase PDI1;1 in actin structures. Microscopic analyses revealed that after Oryza sativa roots were exposed to H2 O2 , both actin and PDI1;1 were depolarized and arranged in a meshwork. In H2 O2 -exposed cells, actin formed intermolecularly disulfide-bonded high-molecular-weight structures, which were thiol-trapped by PDI1;1. Recombinant PDI1;1 exhibited the ability to recognize actin in an in vitro binding assay. During recovery from H2 O2 exposure, the amount of disulfide-bonded high-molecular-weight structures of actin decreased over time, but deficiency of PDI1;1 inhibited the decrease. These results suggest a PDI1;1-dependent pathway that reduces disulfide bonds in high-molecular-weight structures of actin, thus promoting their degradation.
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