ArticlePlant reproduction2020
COPI complex isoforms are required for the early acceptance of compatible pollen grains in Arabidopsis thaliana.
Article in Plant reproduction, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- Arabidopsis TETRASPANIN8 mediates exosome secretion and glycosyl inositol phosphoceramide sorting and trafficking.The Plant cell · 2024Article
- An Overview of Protein Secretion in Plant Cells.Methods in molecular biology (Clifton, N.J.) · 2024Review
- The presence of β'1-COP and β'2-COP is required for female and male gametophyte development.Plant reproduction · 2023Article
- Regulatory dynamics of gene expression in the developing male gametophyte of Arabidopsis.Plant reproduction · 2023Article
- Dynamic Regulation of Lipid Droplet Biogenesis in Plant Cells and Proteins Involved in the Process.International journal of molecular sciences · 2023Review
- Differential Involvement ofCells · 2022Article
- Critical Determinants in ER-Golgi Trafficking of Enzymes Involved in Glycosylation.Plants (Basel, Switzerland) · 2022Review
Corrections and comments
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Authors and funding
7 authors at 1 institution in 2 countries.
Funding
Abstract
The Coat Protein I (COPI) complex is a seven-subunit coatomer complex consisting of the α, β, β', γ, δ, ε, and ζ proteins. In Arabidopsis thaliana, COPI is required for retrograde transport from the Golgi to the endoplasmic reticulum, Golgi maintenance, and cell plate formation. During compatible pollination, vesicle recruitment to the pollen contact point is required for pollen hydration and pollen tube penetration. Here, to identify other aspects of trafficking involved in the acceptance of compatible pollen by stigmatic papillae and to determine their roles in compatible pollination, we characterized knockout lines of several isoforms of the COPI complex, including α1-COP, γ-COP, and ε-COP. Specifically, we characterized pollen grain adherence, pollen tube penetration, and seed set in the mutants. Of the mutant lines examined, α1-cop had the most severe phenotypes, including altered compatible pollen grain adherence and tube germination and reduced seed set, whereas the other lines had milder phenotypes but visibly retarded compatible pollen acceptance. This is the first study demonstrating that COPI complex subunits are required for the acceptance of compatible pollen.
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Registered trials
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