ArticleInternational journal of molecular sciences2013
Environmental stresses induce misfolded protein aggregation in plant cells in a microtubule-dependent manner.
Article in International journal of molecular sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 62 citations in OpenAlex.
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- Detection and Quantification of Protein Aggregates in Plants.Methods in molecular biology (Clifton, N.J.) · 2023Article
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- Molecular Bases of Heat Stress Responses in Vegetable Crops With Focusing on Heat Shock Factors and Heat Shock Proteins.Frontiers in plant science · 2022Review
- β-Cyclocitral, a Master Regulator of Multiple Stress-Responsive Genes inPlants (Basel, Switzerland) · 2021Article
- The intrinsic chaperone network of Arabidopsis stem cells confers protection against proteotoxic stress.Aging cell · 2021Article
- Flavonoids: Potential Candidates for the Treatment of Neurodegenerative Disorders.Biomedicines · 2021Review
- E183K Mutation in Chalcone Synthase C2 Causes Protein Aggregation and Maize Colorless.Frontiers in plant science · 2021Article
- Aggresomal sequestration and STUB1-mediated ubiquitylation during mammalian proteaphagy of inhibited proteasomes.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Control of translation during the unfolded protein response in maize seedlings: Life without PERKs.Plant direct · 2020Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Misfolded protein aggregation in mammalian cells is one of the cellular responses to environmental stresses. However, the aggregation of misfolded proteins in plant cells exposed to environmental stresses is still poorly understood. Here, we report the misfolded protein aggregation in plant cells in response to environmental stresses, including ultraviolet (UV) radiation, heat stress and cold stress. Treatment of grape and tobacco cultured cells with MG-132, a proteasome inhibitor, induced misfolded protein aggregation. All of the environmental stresses examined induced the endoplasmic reticulum (ER) stress response in the cells. The cells under ER stress showed aggregation of misfolded proteins. The misfolded protein aggregation was completely inhibited by treatment of the cells with trichostatin A or colchicine, suggesting that the misfolded proteins might be aggregated in plant cells in a microtubule-dependent manner. Detected aggregates were initially observed immediately after exposure to the environmental stresses (1 min after UV radiation, 5 min after heat stress exposure, and 15 min after cold stress exposure). Based on these findings, we hypothesize that environmental stresses induce misfolded protein aggregation in plant cells in a microtubule-dependent manner.
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