ArticleMicron (Oxford, England : 1993)2017
F-actin reorganization upon de- and rehydration in the aeroterrestrial green alga Klebsormidium crenulatum.
Article in Micron (Oxford, England : 1993), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 10 citations in OpenAlex.
- Detecting Environmental Stress In Situ Using Molecular Data: A Case Study with the Filamentous Green AlgaMicroorganisms · 2025Article
- Phylogenomic insights into the first multicellular streptophyte.Current biology : CB · 2024Article
- The cell biology of charophytes: Exploring the past and models for the future.Plant physiology · 2022Article
- Influencing the Actin Dynamics in Plant Cells by Jasplakinolide, Chondramides, Phalloidin, Cytochalasins, and Latrunculins.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Cold Acclimation Improves the Desiccation Stress Resilience of Polar Strains ofFrontiers in microbiology · 2019Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Filamentous actin (F-actin) is a dynamic network involved in many cellular processes like cell division and cytoplasmic streaming. While many studies have addressed the involvement of F-actin in different cellular processes in cultured cells, little is known on the reactions to environmental stress scenarios, where this system might have essential regulatory functions. We investigated here the de- and rehydration kinetics of breakdown and reassembly of F-actin in the streptophyte green alga Klebsormidium crenulatum. Measurements of the chlorophyll fluorescence (effective quantum yield of photosystem II [ΔF/Fm']) via pulse amplitude modulation were performed as a measure for dehydration induced shut down of physiological activity, which ceased after 141±15min at ∼84% RH. We hypothesized that there is a link between this physiological parameter and the status of the F-actin system. Indeed, 20min of dehydration (ΔF/Fm'=0) leads to a breakdown of the fine cortical F-actin network as visualized by Atto 488 phalloidin staining, and dot-like structures remained. Already 10min after rehydration a beginning reassembly of F-actin is observed, after 25min the F-actin network appeared similar to untreated controls, indicating a full recovery. These results demonstrate the fast kinetics of F-actin dis- and reassembly likely contributing to cellular reorganization upon rehydration.
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