ArticleGenes2023
Proteome and Ubiquitylome Analyses of Maize Endoplasmic Reticulum under Heat Stress.
Article in Genes, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Interactive physiological responses of Vigna radiata L. under combined heat stress and radiofrequency radiation.Protoplasma · 2026Article
- Beyond Protein Abundance: Proteoform Diversity and Phosphoproteome Remodeling in Maize (Proteomes · 2026Review
- Dynamic regulation of proteostasis underlies thermopriming-mediated acquired thermotolerance in Arabidopsis.Plant communications · 2026Article
- ER Proteotoxic Stress Drives Mitochondrial Dysfunction in Heat-Stressed Intestinal Epithelial Cells.Cells · 2026Article
- Combined transcriptomic and proteomic analyses uncover molecular basis of heat tolerance in pakchoi (Frontiers in plant science · 2026Article
- Physiological and molecular responses of individual and combined drought and heat stress on early anthesis of maize (Zea mays L.).Scientific reports · 2025Article
- Genes and pathways correlated with heat stress responses and heat tolerance in maize kernels.Frontiers in plant science · 2023Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
High temperatures severely affect plant growth and pose a threat to global crop production. Heat causes the accumulation of misfolded proteins in the endoplasmic reticulum(ER), as well as triggering the heat-shock response (HSR) in the cytosol and the unfolded protein response (UPR) in the ER. Excessive misfolded proteins undergo further degradation through ER-associated degradation (ERAD). Although much research on the plant heat stress response has been conducted, the regulation of ER-localized proteins has not been well-studied thus far. We isolated the microsome fraction from heat-treated and untreated maize seedlings and performed proteome and ubiquitylome analyses. Of the 8306 total proteins detected in the proteomics analysis, 1675 proteins were significantly up-regulated and 708 proteins were significantly down-regulated. Global ubiquitination analysis revealed 1780 proteins with at least one ubiquitination site. Motif analysis revealed that alanine and glycine are the preferred amino acids upstream and downstream of ubiquitinated lysine sites. ERAD components were found to be hyper-ubiquitinated after heat treatment, implying the feedback regulation of ERAD activity through protein degradation.
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Registered trials
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